2ykn - Revision history

OCA at 07:12, 1 May 2024

OCA — Wed, 01 May 2024 07:12:15 GMT

←Older revision		Revision as of 07:12, 1 May 2024
Line 3:		Line 3:
	<StructureSection load='2ykn' size='340' side='right'caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>		<StructureSection load='2ykn' size='340' side='right'caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Hiv-1 Hiv-~~1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YKN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_BH10 Human immunodeficiency virus type 1 BH10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YKN FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>~~, ~~<scene name='pdbligand=YKN:2-~~[~~DIFLUORO-~~[~~(4-METHYL-PYRIMIDINYL)-THIO~~]~~METHYL~~]~~-BENZOXAZOLE'>YKN</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.12Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[2vg7\|2vg7]]~~, [[1ajv\|1ajv]], [[1har\|1har]], [[1hps\|1hps]], [[1t7k\|1t7k]], [[1d4j\|1d4j]], [[1r0a\|1r0a]], [[1hpz\|1hpz]], [[2vg6\|2vg6]], [[1hqe\|1hqe]], [[1qe1\|1qe1]], [[1npa\|1npa]], [[1ajx\|1ajx]], [[1ebk\|1ebk]], [[1tvr\|1tvr]], [[1s6p\|1s6p]], [[1ikv\|1ikv]], [[1bqm\|1bqm]], [[1w5y\|1w5y]], [[1hos\|1hos]], [[1ikw\|1ikw]], [[1s6q\|1s6q]], [[3hvt\|3hvt]], [[1ec1\|1ec1]], [[1ec0\|1ec0]], [[2xyf\|2xyf]], [[1t05\|1t05]], [[1rvq\|1rvq]], [[1d4i\|1d4i]], [[1meu\|1meu]], [[1s9g\|1s9g]], [[2be2\|2be2]], [[1hnv\|1hnv]], [[1rvr\|1rvr]], [[1ikx\|1ikx]], [[1w5w\|1w5w]], [[1iky\|1iky]], [[1qmc\|1qmc]], [[1n6q\|1n6q]], [[1d4h\|1d4h]], [[1rvn\|1rvn]], [[1hbv\|1hbv]], [[1htf\|1htf]], [[1rtd\|1rtd]], [[1ec2\|1ec2]], [[2hmi\|2hmi]], [[1w5v\|1w5v]], [[1sv5\|1sv5]], [[2uy0\|2uy0]], [[1hmv\|1hmv]], [[2bbb\|2bbb]], [[1s9e\|1s9e]], [[2x4u\|2x4u]], [[1n5y\|1n5y]], [[1dlo\|1dlo]], [[1heg\|1heg]], [[1rvp\|1rvp]], [[1rvl\|1rvl]], [[1dw6\|1dw6]], [[1eet\|1eet]], [[1w5x\|1w5x]], [[1yt9\|1yt9]], [[2b6a\|2b6a]], [[1htg\|1htg]], [[1hvu\|1hvu]], [[1ebw\|1ebw]], [[2ban\|2ban]], [[1rdh\|1rdh]], [[2xye\|2xye]], [[1eby\|1eby]], [[1j5o\|1j5o]], [[1rvo\|1rvo]], [[1hvp\|1hvp]], [[1mes\|1mes]], [[1ec3\|1ec3]], [[1hef\|1hef]], [[1hih\|1hih]], [[1hni\|1hni]], [[1tv6\|1tv6]], [[1a9m\|1a9m]], [[1ebz\|1ebz]], [[2b5j\|2b5j]], [[1hys\|1hys]], [[1met\|1met]], [[1t03\|1t03]], [[1axa\|1axa]], [[1mer\|1mer]], [[1npw\|1npw]], [[3tlh\|3tlh]], [[1suq\|1suq]], [[2uxz\|2uxz]], [[1hvk\|1hvk]], [[1sbg\|1sbg]], [[1bqn\|1bqn]], [[1uwb\|1uwb]], [[2vg5\|2vg5]], [[1rvm\|1rvm]], [[1hte\|1hte]], [[1hrh\|1hrh]], [[1npv\|1npv]], [[1hqu\|1hqu]], [[2ykm\|2ykm]]</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YKN:2-[DIFLUORO-[(4-METHYL-PYRIMIDINYL)-THIO]METHYL]-BENZOXAZOLE'>YKN</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [https://pdbe.org/2ykn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [https://www.ebi.ac.uk/pdbsum/2ykn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykn ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [https://pdbe.org/2ykn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [https://www.ebi.ac.uk/pdbsum/2ykn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/POL_HV1B1 POL_HV1B1]] Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity).<ref>PMID:9658129</ref> Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to play a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. It binds in the cytoplasm the human BAF protein which prevent autointegration of the viral genome, and might be included in virions at the ration of zero to 3 BAF dimer per virion. The myristoylation signal and the NLS thus exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity).<ref>PMID:9658129</ref> Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (By similarity).<ref>PMID:9658129</ref> Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity).<ref>PMID:9658129</ref> The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (By similarity).<ref>PMID:9658129</ref> Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).<ref>PMID:9658129</ref> Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity).<ref>PMID:9658129</ref>	+	[https://www.uniprot.org/uniprot/POL_HV1B1 POL_HV1B1] Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity).<ref>PMID:9658129</ref> Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to play a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. It binds in the cytoplasm the human BAF protein which prevent autointegration of the viral genome, and might be included in virions at the ration of zero to 3 BAF dimer per virion. The myristoylation signal and the NLS thus exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity).<ref>PMID:9658129</ref> Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (By similarity).<ref>PMID:9658129</ref> Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity).<ref>PMID:9658129</ref> The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (By similarity).<ref>PMID:9658129</ref> Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).<ref>PMID:9658129</ref> Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity).<ref>PMID:9658129</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	This paper reports the synthesis and antiviral properties of new difluoromethylbenzoxazole (DFMB) pyrimidine thioether derivatives as non-nucleoside HIV-1 reverse transcriptase inhibitors. By use of a combination of structural biology study and traditional medicinal chemistry, several members of this novel class were synthesized using a single electron transfer chain process (radical nucleophilic substitution, S(RN)1) and were found to be potent against wild-type HIV-1 reverse transcriptase, with low cytotoxicity but with moderate activity against drug-resistant strains. The most promising compound 24 showed a significant EC(50) value close to 6.4 nM against HIV-1 IIIB, a moderate EC(50) value close to 54 muM against an NNRTI resistant double mutant (K103N + Y181C), but an excellent selectivity index >15477 (CC(50) > 100 muM).	+
-		+
-	Difluoromethylbenzoxazole Pyrimidine Thioether Derivatives: A Novel Class of Potent Non-Nucleoside HIV-1 Reverse Transcriptase Inhibitors.,Boyer J, Arnoult E, Medebielle M, Guillemont J, Unge J, Jochmans D J Med Chem. 2011 Dec 8;54(23):7974-85. Epub 2011 Nov 4. PMID:22017513<ref>PMID:22017513</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 2ykn" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 26:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Hiv-~~1]]	+	[[Category: Human immunodeficiency virus type 1 BH10]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arnoult, E]]	+	[[Category: Arnoult E]]
-	[[Category: Boyer, J]]	+	[[Category: Boyer J]]
-	[[Category: Guillemont, J]]	+	[[Category: Guillemont J]]
-	[[Category: Jochmans, D]]	+	[[Category: Jochmans D]]
-	[[Category: Medebielle, M]]	+	[[Category: Medebielle M]]
-	[[Category: Unge, J]]	+	[[Category: Unge J]]
-	[[Category: Unge, T]]	+	[[Category: Unge T]]
-	~~[[Category: Hydrolase~~]]	+

OCA at 05:26, 25 August 2022

OCA — Thu, 25 Aug 2022 05:26:53 GMT

←Older revision		Revision as of 05:26, 25 August 2022
Line 3:		Line 3:
	<StructureSection load='2ykn' size='340' side='right'caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>		<StructureSection load='2ykn' size='340' side='right'caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Hiv-1 Hiv-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2YKN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hiv-1 Hiv-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YKN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YKN:2-[DIFLUORO-[(4-METHYL-PYRIMIDINYL)-THIO]METHYL]-BENZOXAZOLE'>YKN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YKN:2-[DIFLUORO-[(4-METHYL-PYRIMIDINYL)-THIO]METHYL]-BENZOXAZOLE'>YKN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vg7\|2vg7]], [[1ajv\|1ajv]], [[1har\|1har]], [[1hps\|1hps]], [[1t7k\|1t7k]], [[1d4j\|1d4j]], [[1r0a\|1r0a]], [[1hpz\|1hpz]], [[2vg6\|2vg6]], [[1hqe\|1hqe]], [[1qe1\|1qe1]], [[1npa\|1npa]], [[1ajx\|1ajx]], [[1ebk\|1ebk]], [[1tvr\|1tvr]], [[1s6p\|1s6p]], [[1ikv\|1ikv]], [[1bqm\|1bqm]], [[1w5y\|1w5y]], [[1hos\|1hos]], [[1ikw\|1ikw]], [[1s6q\|1s6q]], [[3hvt\|3hvt]], [[1ec1\|1ec1]], [[1ec0\|1ec0]], [[2xyf\|2xyf]], [[1t05\|1t05]], [[1rvq\|1rvq]], [[1d4i\|1d4i]], [[1meu\|1meu]], [[1s9g\|1s9g]], [[2be2\|2be2]], [[1hnv\|1hnv]], [[1rvr\|1rvr]], [[1ikx\|1ikx]], [[1w5w\|1w5w]], [[1iky\|1iky]], [[1qmc\|1qmc]], [[1n6q\|1n6q]], [[1d4h\|1d4h]], [[1rvn\|1rvn]], [[1hbv\|1hbv]], [[1htf\|1htf]], [[1rtd\|1rtd]], [[1ec2\|1ec2]], [[2hmi\|2hmi]], [[1w5v\|1w5v]], [[1sv5\|1sv5]], [[2uy0\|2uy0]], [[1hmv\|1hmv]], [[2bbb\|2bbb]], [[1s9e\|1s9e]], [[2x4u\|2x4u]], [[1n5y\|1n5y]], [[1dlo\|1dlo]], [[1heg\|1heg]], [[1rvp\|1rvp]], [[1rvl\|1rvl]], [[1dw6\|1dw6]], [[1eet\|1eet]], [[1w5x\|1w5x]], [[1yt9\|1yt9]], [[2b6a\|2b6a]], [[1htg\|1htg]], [[1hvu\|1hvu]], [[1ebw\|1ebw]], [[2ban\|2ban]], [[1rdh\|1rdh]], [[2xye\|2xye]], [[1eby\|1eby]], [[1j5o\|1j5o]], [[1rvo\|1rvo]], [[1hvp\|1hvp]], [[1mes\|1mes]], [[1ec3\|1ec3]], [[1hef\|1hef]], [[1hih\|1hih]], [[1hni\|1hni]], [[1tv6\|1tv6]], [[1a9m\|1a9m]], [[1ebz\|1ebz]], [[2b5j\|2b5j]], [[1hys\|1hys]], [[1met\|1met]], [[1t03\|1t03]], [[1axa\|1axa]], [[1mer\|1mer]], [[1npw\|1npw]], [[3tlh\|3tlh]], [[1suq\|1suq]], [[2uxz\|2uxz]], [[1hvk\|1hvk]], [[1sbg\|1sbg]], [[1bqn\|1bqn]], [[1uwb\|1uwb]], [[2vg5\|2vg5]], [[1rvm\|1rvm]], [[1hte\|1hte]], [[1hrh\|1hrh]], [[1npv\|1npv]], [[1hqu\|1hqu]], [[2ykm\|2ykm]]</div></td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vg7\|2vg7]], [[1ajv\|1ajv]], [[1har\|1har]], [[1hps\|1hps]], [[1t7k\|1t7k]], [[1d4j\|1d4j]], [[1r0a\|1r0a]], [[1hpz\|1hpz]], [[2vg6\|2vg6]], [[1hqe\|1hqe]], [[1qe1\|1qe1]], [[1npa\|1npa]], [[1ajx\|1ajx]], [[1ebk\|1ebk]], [[1tvr\|1tvr]], [[1s6p\|1s6p]], [[1ikv\|1ikv]], [[1bqm\|1bqm]], [[1w5y\|1w5y]], [[1hos\|1hos]], [[1ikw\|1ikw]], [[1s6q\|1s6q]], [[3hvt\|3hvt]], [[1ec1\|1ec1]], [[1ec0\|1ec0]], [[2xyf\|2xyf]], [[1t05\|1t05]], [[1rvq\|1rvq]], [[1d4i\|1d4i]], [[1meu\|1meu]], [[1s9g\|1s9g]], [[2be2\|2be2]], [[1hnv\|1hnv]], [[1rvr\|1rvr]], [[1ikx\|1ikx]], [[1w5w\|1w5w]], [[1iky\|1iky]], [[1qmc\|1qmc]], [[1n6q\|1n6q]], [[1d4h\|1d4h]], [[1rvn\|1rvn]], [[1hbv\|1hbv]], [[1htf\|1htf]], [[1rtd\|1rtd]], [[1ec2\|1ec2]], [[2hmi\|2hmi]], [[1w5v\|1w5v]], [[1sv5\|1sv5]], [[2uy0\|2uy0]], [[1hmv\|1hmv]], [[2bbb\|2bbb]], [[1s9e\|1s9e]], [[2x4u\|2x4u]], [[1n5y\|1n5y]], [[1dlo\|1dlo]], [[1heg\|1heg]], [[1rvp\|1rvp]], [[1rvl\|1rvl]], [[1dw6\|1dw6]], [[1eet\|1eet]], [[1w5x\|1w5x]], [[1yt9\|1yt9]], [[2b6a\|2b6a]], [[1htg\|1htg]], [[1hvu\|1hvu]], [[1ebw\|1ebw]], [[2ban\|2ban]], [[1rdh\|1rdh]], [[2xye\|2xye]], [[1eby\|1eby]], [[1j5o\|1j5o]], [[1rvo\|1rvo]], [[1hvp\|1hvp]], [[1mes\|1mes]], [[1ec3\|1ec3]], [[1hef\|1hef]], [[1hih\|1hih]], [[1hni\|1hni]], [[1tv6\|1tv6]], [[1a9m\|1a9m]], [[1ebz\|1ebz]], [[2b5j\|2b5j]], [[1hys\|1hys]], [[1met\|1met]], [[1t03\|1t03]], [[1axa\|1axa]], [[1mer\|1mer]], [[1npw\|1npw]], [[3tlh\|3tlh]], [[1suq\|1suq]], [[2uxz\|2uxz]], [[1hvk\|1hvk]], [[1sbg\|1sbg]], [[1bqn\|1bqn]], [[1uwb\|1uwb]], [[2vg5\|2vg5]], [[1rvm\|1rvm]], [[1hte\|1hte]], [[1hrh\|1hrh]], [[1npv\|1npv]], [[1hqu\|1hqu]], [[2ykm\|2ykm]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [~~http~~://pdbe.org/2ykn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2ykn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykn ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [https://pdbe.org/2ykn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [https://www.ebi.ac.uk/pdbsum/2ykn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/POL_HV1B1 POL_HV1B1]] Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity).<ref>PMID:9658129</ref> Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to play a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. It binds in the cytoplasm the human BAF protein which prevent autointegration of the viral genome, and might be included in virions at the ration of zero to 3 BAF dimer per virion. The myristoylation signal and the NLS thus exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity).<ref>PMID:9658129</ref> Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (By similarity).<ref>PMID:9658129</ref> Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity).<ref>PMID:9658129</ref> The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (By similarity).<ref>PMID:9658129</ref> Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).<ref>PMID:9658129</ref> Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity).<ref>PMID:9658129</ref>	+	[[https://www.uniprot.org/uniprot/POL_HV1B1 POL_HV1B1]] Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity).<ref>PMID:9658129</ref> Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to play a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. It binds in the cytoplasm the human BAF protein which prevent autointegration of the viral genome, and might be included in virions at the ration of zero to 3 BAF dimer per virion. The myristoylation signal and the NLS thus exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity).<ref>PMID:9658129</ref> Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (By similarity).<ref>PMID:9658129</ref> Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity).<ref>PMID:9658129</ref> The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (By similarity).<ref>PMID:9658129</ref> Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).<ref>PMID:9658129</ref> Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity).<ref>PMID:9658129</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 05:07, 19 November 2020

OCA — Thu, 19 Nov 2020 05:07:41 GMT

←Older revision		Revision as of 05:07, 19 November 2020
Line 3:		Line 3:
	<StructureSection load='2ykn' size='340' side='right'caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>		<StructureSection load='2ykn' size='340' side='right'caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hiv-1 Hiv-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2YKN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hiv-1 Hiv-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2YKN FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YKN:2-[DIFLUORO-[(4-METHYL-PYRIMIDINYL)-THIO]METHYL]-BENZOXAZOLE'>YKN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YKN:2-[DIFLUORO-[(4-METHYL-PYRIMIDINYL)-THIO]METHYL]-BENZOXAZOLE'>YKN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vg7\|2vg7]], [[1ajv\|1ajv]], [[1har\|1har]], [[1hps\|1hps]], [[1t7k\|1t7k]], [[1d4j\|1d4j]], [[1r0a\|1r0a]], [[1hpz\|1hpz]], [[2vg6\|2vg6]], [[1hqe\|1hqe]], [[1qe1\|1qe1]], [[1npa\|1npa]], [[1ajx\|1ajx]], [[1ebk\|1ebk]], [[1tvr\|1tvr]], [[1s6p\|1s6p]], [[1ikv\|1ikv]], [[1bqm\|1bqm]], [[1w5y\|1w5y]], [[1hos\|1hos]], [[1ikw\|1ikw]], [[1s6q\|1s6q]], [[3hvt\|3hvt]], [[1ec1\|1ec1]], [[1ec0\|1ec0]], [[2xyf\|2xyf]], [[1t05\|1t05]], [[1rvq\|1rvq]], [[1d4i\|1d4i]], [[1meu\|1meu]], [[1s9g\|1s9g]], [[2be2\|2be2]], [[1hnv\|1hnv]], [[1rvr\|1rvr]], [[1ikx\|1ikx]], [[1w5w\|1w5w]], [[1iky\|1iky]], [[1qmc\|1qmc]], [[1n6q\|1n6q]], [[1d4h\|1d4h]], [[1rvn\|1rvn]], [[1hbv\|1hbv]], [[1htf\|1htf]], [[1rtd\|1rtd]], [[1ec2\|1ec2]], [[2hmi\|2hmi]], [[1w5v\|1w5v]], [[1sv5\|1sv5]], [[2uy0\|2uy0]], [[1hmv\|1hmv]], [[2bbb\|2bbb]], [[1s9e\|1s9e]], [[2x4u\|2x4u]], [[1n5y\|1n5y]], [[1dlo\|1dlo]], [[1heg\|1heg]], [[1rvp\|1rvp]], [[1rvl\|1rvl]], [[1dw6\|1dw6]], [[1eet\|1eet]], [[1w5x\|1w5x]], [[1yt9\|1yt9]], [[2b6a\|2b6a]], [[1htg\|1htg]], [[1hvu\|1hvu]], [[1ebw\|1ebw]], [[2ban\|2ban]], [[1rdh\|1rdh]], [[2xye\|2xye]], [[1eby\|1eby]], [[1j5o\|1j5o]], [[1rvo\|1rvo]], [[1hvp\|1hvp]], [[1mes\|1mes]], [[1ec3\|1ec3]], [[1hef\|1hef]], [[1hih\|1hih]], [[1hni\|1hni]], [[1tv6\|1tv6]], [[1a9m\|1a9m]], [[1ebz\|1ebz]], [[2b5j\|2b5j]], [[1hys\|1hys]], [[1met\|1met]], [[1t03\|1t03]], [[1axa\|1axa]], [[1mer\|1mer]], [[1npw\|1npw]], [[3tlh\|3tlh]], [[1suq\|1suq]], [[2uxz\|2uxz]], [[1hvk\|1hvk]], [[1sbg\|1sbg]], [[1bqn\|1bqn]], [[1uwb\|1uwb]], [[2vg5\|2vg5]], [[1rvm\|1rvm]], [[1hte\|1hte]], [[1hrh\|1hrh]], [[1npv\|1npv]], [[1hqu\|1hqu]], [[2ykm\|2ykm]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vg7\|2vg7]], [[1ajv\|1ajv]], [[1har\|1har]], [[1hps\|1hps]], [[1t7k\|1t7k]], [[1d4j\|1d4j]], [[1r0a\|1r0a]], [[1hpz\|1hpz]], [[2vg6\|2vg6]], [[1hqe\|1hqe]], [[1qe1\|1qe1]], [[1npa\|1npa]], [[1ajx\|1ajx]], [[1ebk\|1ebk]], [[1tvr\|1tvr]], [[1s6p\|1s6p]], [[1ikv\|1ikv]], [[1bqm\|1bqm]], [[1w5y\|1w5y]], [[1hos\|1hos]], [[1ikw\|1ikw]], [[1s6q\|1s6q]], [[3hvt\|3hvt]], [[1ec1\|1ec1]], [[1ec0\|1ec0]], [[2xyf\|2xyf]], [[1t05\|1t05]], [[1rvq\|1rvq]], [[1d4i\|1d4i]], [[1meu\|1meu]], [[1s9g\|1s9g]], [[2be2\|2be2]], [[1hnv\|1hnv]], [[1rvr\|1rvr]], [[1ikx\|1ikx]], [[1w5w\|1w5w]], [[1iky\|1iky]], [[1qmc\|1qmc]], [[1n6q\|1n6q]], [[1d4h\|1d4h]], [[1rvn\|1rvn]], [[1hbv\|1hbv]], [[1htf\|1htf]], [[1rtd\|1rtd]], [[1ec2\|1ec2]], [[2hmi\|2hmi]], [[1w5v\|1w5v]], [[1sv5\|1sv5]], [[2uy0\|2uy0]], [[1hmv\|1hmv]], [[2bbb\|2bbb]], [[1s9e\|1s9e]], [[2x4u\|2x4u]], [[1n5y\|1n5y]], [[1dlo\|1dlo]], [[1heg\|1heg]], [[1rvp\|1rvp]], [[1rvl\|1rvl]], [[1dw6\|1dw6]], [[1eet\|1eet]], [[1w5x\|1w5x]], [[1yt9\|1yt9]], [[2b6a\|2b6a]], [[1htg\|1htg]], [[1hvu\|1hvu]], [[1ebw\|1ebw]], [[2ban\|2ban]], [[1rdh\|1rdh]], [[2xye\|2xye]], [[1eby\|1eby]], [[1j5o\|1j5o]], [[1rvo\|1rvo]], [[1hvp\|1hvp]], [[1mes\|1mes]], [[1ec3\|1ec3]], [[1hef\|1hef]], [[1hih\|1hih]], [[1hni\|1hni]], [[1tv6\|1tv6]], [[1a9m\|1a9m]], [[1ebz\|1ebz]], [[2b5j\|2b5j]], [[1hys\|1hys]], [[1met\|1met]], [[1t03\|1t03]], [[1axa\|1axa]], [[1mer\|1mer]], [[1npw\|1npw]], [[3tlh\|3tlh]], [[1suq\|1suq]], [[2uxz\|2uxz]], [[1hvk\|1hvk]], [[1sbg\|1sbg]], [[1bqn\|1bqn]], [[1uwb\|1uwb]], [[2vg5\|2vg5]], [[1rvm\|1rvm]], [[1hte\|1hte]], [[1hrh\|1hrh]], [[1npv\|1npv]], [[1hqu\|1hqu]], [[2ykm\|2ykm]]</div></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [http://pdbe.org/2ykn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [http://www.ebi.ac.uk/pdbsum/2ykn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykn ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [http://pdbe.org/2ykn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [http://www.ebi.ac.uk/pdbsum/2ykn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 13:49, 25 December 2019

OCA — Wed, 25 Dec 2019 13:49:43 GMT

←Older revision		Revision as of 13:49, 25 December 2019
Line 1:		Line 1:

	==Crystal structure of HIV-1 Reverse Transcriptase (RT) in complex with a Difluoromethylbenzoxazole (DFMB) Pyrimidine Thioether derivative, a non-nucleoside RT inhibitor (NNRTI)==		==Crystal structure of HIV-1 Reverse Transcriptase (RT) in complex with a Difluoromethylbenzoxazole (DFMB) Pyrimidine Thioether derivative, a non-nucleoside RT inhibitor (NNRTI)==
-	<StructureSection load='2ykn' size='340' side='right' caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>	+	<StructureSection load='2ykn' size='340' side='right'caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hiv-1 Hiv-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YKN FirstGlance]. <br>		<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hiv-1 Hiv-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YKN FirstGlance]. <br>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 2ykn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2ykn" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Reverse transcriptase 3D structures\|Reverse transcriptase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Hiv-1]]		[[Category: Hiv-1]]
		+	[[Category: Large Structures]]
	[[Category: Arnoult, E]]		[[Category: Arnoult, E]]
	[[Category: Boyer, J]]		[[Category: Boyer, J]]

OCA at 07:34, 17 January 2018

OCA — Wed, 17 Jan 2018 07:34:35 GMT

←Older revision		Revision as of 07:34, 17 January 2018
Line 1:		Line 1:

-	==~~CRYSTAL STRUCTURE OF~~ HIV-1 ~~REVERSE TRANSCRIPTASE~~ (RT) ~~IN COMPLEX WITH A DIFLUOROMETHYLBENZOXAZOLE~~ (DFMB) ~~PYRIMIDINE THIOETHER DERIVATIVE~~, ~~A NON~~-~~NUCLEOSIDE~~ RT ~~INHIBITOR~~ (NNRTI)==	+	==Crystal structure of HIV-1 Reverse Transcriptase (RT) in complex with a Difluoromethylbenzoxazole (DFMB) Pyrimidine Thioether derivative, a non-nucleoside RT inhibitor (NNRTI)==
	<StructureSection load='2ykn' size='340' side='right' caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>		<StructureSection load='2ykn' size='340' side='right' caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 2ykn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2ykn" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Reverse transcriptase\|Reverse transcriptase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 14:47, 5 August 2016

OCA — Fri, 05 Aug 2016 14:47:14 GMT

←Older revision		Revision as of 14:47, 5 August 2016
Line 1:		Line 1:
		+
	==CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) IN COMPLEX WITH A DIFLUOROMETHYLBENZOXAZOLE (DFMB) PYRIMIDINE THIOETHER DERIVATIVE, A NON-NUCLEOSIDE RT INHIBITOR (NNRTI)==		==CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) IN COMPLEX WITH A DIFLUOROMETHYLBENZOXAZOLE (DFMB) PYRIMIDINE THIOETHER DERIVATIVE, A NON-NUCLEOSIDE RT INHIBITOR (NNRTI)==
	<StructureSection load='2ykn' size='340' side='right' caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>		<StructureSection load='2ykn' size='340' side='right' caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Human_immunodeficiency_virus_type_1_bh10 Human immunodeficiency virus type~~ 1 ~~bh10~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YKN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hiv-1 Hiv-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YKN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YKN:2-[DIFLUORO-[(4-METHYL-PYRIMIDINYL)-THIO]METHYL]-BENZOXAZOLE'>YKN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YKN:2-[DIFLUORO-[(4-METHYL-PYRIMIDINYL)-THIO]METHYL]-BENZOXAZOLE'>YKN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vg7\|2vg7]], [[1ajv\|1ajv]], [[1har\|1har]], [[1hps\|1hps]], [[1t7k\|1t7k]], [[1d4j\|1d4j]], [[1r0a\|1r0a]], [[1hpz\|1hpz]], [[2vg6\|2vg6]], [[1hqe\|1hqe]], [[1qe1\|1qe1]], [[1npa\|1npa]], [[1ajx\|1ajx]], [[1ebk\|1ebk]], [[1tvr\|1tvr]], [[1s6p\|1s6p]], [[1ikv\|1ikv]], [[1bqm\|1bqm]], [[1w5y\|1w5y]], [[1hos\|1hos]], [[1ikw\|1ikw]], [[1s6q\|1s6q]], [[3hvt\|3hvt]], [[1ec1\|1ec1]], [[1ec0\|1ec0]], [[2xyf\|2xyf]], [[1t05\|1t05]], [[1rvq\|1rvq]], [[1d4i\|1d4i]], [[1meu\|1meu]], [[1s9g\|1s9g]], [[2be2\|2be2]], [[1hnv\|1hnv]], [[1rvr\|1rvr]], [[1ikx\|1ikx]], [[1w5w\|1w5w]], [[1iky\|1iky]], [[1qmc\|1qmc]], [[1n6q\|1n6q]], [[1d4h\|1d4h]], [[1rvn\|1rvn]], [[1hbv\|1hbv]], [[1htf\|1htf]], [[1rtd\|1rtd]], [[1ec2\|1ec2]], [[2hmi\|2hmi]], [[1w5v\|1w5v]], [[1sv5\|1sv5]], [[2uy0\|2uy0]], [[1hmv\|1hmv]], [[2bbb\|2bbb]], [[1s9e\|1s9e]], [[2x4u\|2x4u]], [[1n5y\|1n5y]], [[1dlo\|1dlo]], [[1heg\|1heg]], [[1rvp\|1rvp]], [[1rvl\|1rvl]], [[1dw6\|1dw6]], [[1eet\|1eet]], [[1w5x\|1w5x]], [[1yt9\|1yt9]], [[2b6a\|2b6a]], [[1htg\|1htg]], [[1hvu\|1hvu]], [[1ebw\|1ebw]], [[2ban\|2ban]], [[1rdh\|1rdh]], [[2xye\|2xye]], [[1eby\|1eby]], [[1j5o\|1j5o]], [[1rvo\|1rvo]], [[1hvp\|1hvp]], [[1mes\|1mes]], [[1ec3\|1ec3]], [[1hef\|1hef]], [[1hih\|1hih]], [[1hni\|1hni]], [[1tv6\|1tv6]], [[1a9m\|1a9m]], [[1ebz\|1ebz]], [[2b5j\|2b5j]], [[1hys\|1hys]], [[1met\|1met]], [[1t03\|1t03]], [[1axa\|1axa]], [[1mer\|1mer]], [[1npw\|1npw]], [[3tlh\|3tlh]], [[1suq\|1suq]], [[2uxz\|2uxz]], [[1hvk\|1hvk]], [[1sbg\|1sbg]], [[1bqn\|1bqn]], [[1uwb\|1uwb]], [[2vg5\|2vg5]], [[1rvm\|1rvm]], [[1hte\|1hte]], [[1hrh\|1hrh]], [[1npv\|1npv]], [[1hqu\|1hqu]], [[2ykm\|2ykm]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vg7\|2vg7]], [[1ajv\|1ajv]], [[1har\|1har]], [[1hps\|1hps]], [[1t7k\|1t7k]], [[1d4j\|1d4j]], [[1r0a\|1r0a]], [[1hpz\|1hpz]], [[2vg6\|2vg6]], [[1hqe\|1hqe]], [[1qe1\|1qe1]], [[1npa\|1npa]], [[1ajx\|1ajx]], [[1ebk\|1ebk]], [[1tvr\|1tvr]], [[1s6p\|1s6p]], [[1ikv\|1ikv]], [[1bqm\|1bqm]], [[1w5y\|1w5y]], [[1hos\|1hos]], [[1ikw\|1ikw]], [[1s6q\|1s6q]], [[3hvt\|3hvt]], [[1ec1\|1ec1]], [[1ec0\|1ec0]], [[2xyf\|2xyf]], [[1t05\|1t05]], [[1rvq\|1rvq]], [[1d4i\|1d4i]], [[1meu\|1meu]], [[1s9g\|1s9g]], [[2be2\|2be2]], [[1hnv\|1hnv]], [[1rvr\|1rvr]], [[1ikx\|1ikx]], [[1w5w\|1w5w]], [[1iky\|1iky]], [[1qmc\|1qmc]], [[1n6q\|1n6q]], [[1d4h\|1d4h]], [[1rvn\|1rvn]], [[1hbv\|1hbv]], [[1htf\|1htf]], [[1rtd\|1rtd]], [[1ec2\|1ec2]], [[2hmi\|2hmi]], [[1w5v\|1w5v]], [[1sv5\|1sv5]], [[2uy0\|2uy0]], [[1hmv\|1hmv]], [[2bbb\|2bbb]], [[1s9e\|1s9e]], [[2x4u\|2x4u]], [[1n5y\|1n5y]], [[1dlo\|1dlo]], [[1heg\|1heg]], [[1rvp\|1rvp]], [[1rvl\|1rvl]], [[1dw6\|1dw6]], [[1eet\|1eet]], [[1w5x\|1w5x]], [[1yt9\|1yt9]], [[2b6a\|2b6a]], [[1htg\|1htg]], [[1hvu\|1hvu]], [[1ebw\|1ebw]], [[2ban\|2ban]], [[1rdh\|1rdh]], [[2xye\|2xye]], [[1eby\|1eby]], [[1j5o\|1j5o]], [[1rvo\|1rvo]], [[1hvp\|1hvp]], [[1mes\|1mes]], [[1ec3\|1ec3]], [[1hef\|1hef]], [[1hih\|1hih]], [[1hni\|1hni]], [[1tv6\|1tv6]], [[1a9m\|1a9m]], [[1ebz\|1ebz]], [[2b5j\|2b5j]], [[1hys\|1hys]], [[1met\|1met]], [[1t03\|1t03]], [[1axa\|1axa]], [[1mer\|1mer]], [[1npw\|1npw]], [[3tlh\|3tlh]], [[1suq\|1suq]], [[2uxz\|2uxz]], [[1hvk\|1hvk]], [[1sbg\|1sbg]], [[1bqn\|1bqn]], [[1uwb\|1uwb]], [[2vg5\|2vg5]], [[1rvm\|1rvm]], [[1hte\|1hte]], [[1hrh\|1hrh]], [[1npv\|1npv]], [[1hqu\|1hqu]], [[2ykm\|2ykm]]</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [http://www.ebi.ac.uk/pdbsum/2ykn PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [http://pdbe.org/2ykn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [http://www.ebi.ac.uk/pdbsum/2ykn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ykn ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 2ykn" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Reverse transcriptase\|Reverse transcriptase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human immunodeficiency virus type~~ 1 ~~bh10~~]]	+	[[Category: Hiv-1]]
	[[Category: Arnoult, E]]		[[Category: Arnoult, E]]
	[[Category: Boyer, J]]		[[Category: Boyer, J]]

OCA at 19:41, 25 December 2014

OCA — Thu, 25 Dec 2014 19:41:32 GMT

←Older revision		Revision as of 19:41, 25 December 2014
Line 2:		Line 2:
	<StructureSection load='2ykn' size='340' side='right' caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>		<StructureSection load='2ykn' size='340' side='right' caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_bh10 Human immunodeficiency virus type 1 bh10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. <br>	+	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_bh10 Human immunodeficiency virus type 1 bh10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YKN FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YKN:2-[DIFLUORO-[(4-METHYL-PYRIMIDINYL)-THIO]METHYL]-BENZOXAZOLE'>YKN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YKN:2-[DIFLUORO-[(4-METHYL-PYRIMIDINYL)-THIO]METHYL]-BENZOXAZOLE'>YKN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vg7\|2vg7]], [[1ajv\|1ajv]], [[1har\|1har]], [[1hps\|1hps]], [[1t7k\|1t7k]], [[1d4j\|1d4j]], [[1r0a\|1r0a]], [[1hpz\|1hpz]], [[2vg6\|2vg6]], [[1hqe\|1hqe]], [[1qe1\|1qe1]], [[1npa\|1npa]], [[1ajx\|1ajx]], [[1ebk\|1ebk]], [[1tvr\|1tvr]], [[1s6p\|1s6p]], [[1ikv\|1ikv]], [[1bqm\|1bqm]], [[1w5y\|1w5y]], [[1hos\|1hos]], [[1ikw\|1ikw]], [[1s6q\|1s6q]], [[3hvt\|3hvt]], [[1ec1\|1ec1]], [[1ec0\|1ec0]], [[2xyf\|2xyf]], [[1t05\|1t05]], [[1rvq\|1rvq]], [[1d4i\|1d4i]], [[1meu\|1meu]], [[1s9g\|1s9g]], [[2be2\|2be2]], [[1hnv\|1hnv]], [[1rvr\|1rvr]], [[1ikx\|1ikx]], [[1w5w\|1w5w]], [[1iky\|1iky]], [[1qmc\|1qmc]], [[1n6q\|1n6q]], [[1d4h\|1d4h]], [[1rvn\|1rvn]], [[1hbv\|1hbv]], [[1htf\|1htf]], [[1rtd\|1rtd]], [[1ec2\|1ec2]], [[2hmi\|2hmi]], [[1w5v\|1w5v]], [[1sv5\|1sv5]], [[2uy0\|2uy0]], [[1hmv\|1hmv]], [[2bbb\|2bbb]], [[1s9e\|1s9e]], [[2x4u\|2x4u]], [[1n5y\|1n5y]], [[1dlo\|1dlo]], [[1heg\|1heg]], [[1rvp\|1rvp]], [[1rvl\|1rvl]], [[1dw6\|1dw6]], [[1eet\|1eet]], [[1w5x\|1w5x]], [[1yt9\|1yt9]], [[2b6a\|2b6a]], [[1htg\|1htg]], [[1hvu\|1hvu]], [[1ebw\|1ebw]], [[2ban\|2ban]], [[1rdh\|1rdh]], [[2xye\|2xye]], [[1eby\|1eby]], [[1j5o\|1j5o]], [[1rvo\|1rvo]], [[1hvp\|1hvp]], [[1mes\|1mes]], [[1ec3\|1ec3]], [[1hef\|1hef]], [[1hih\|1hih]], [[1hni\|1hni]], [[1tv6\|1tv6]], [[1a9m\|1a9m]], [[1ebz\|1ebz]], [[2b5j\|2b5j]], [[1hys\|1hys]], [[1met\|1met]], [[1t03\|1t03]], [[1axa\|1axa]], [[1mer\|1mer]], [[1npw\|1npw]], [[3tlh\|3tlh]], [[1suq\|1suq]], [[2uxz\|2uxz]], [[1hvk\|1hvk]], [[1sbg\|1sbg]], [[1bqn\|1bqn]], [[1uwb\|1uwb]], [[2vg5\|2vg5]], [[1rvm\|1rvm]], [[1hte\|1hte]], [[1hrh\|1hrh]], [[1npv\|1npv]], [[1hqu\|1hqu]], [[2ykm\|2ykm]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vg7\|2vg7]], [[1ajv\|1ajv]], [[1har\|1har]], [[1hps\|1hps]], [[1t7k\|1t7k]], [[1d4j\|1d4j]], [[1r0a\|1r0a]], [[1hpz\|1hpz]], [[2vg6\|2vg6]], [[1hqe\|1hqe]], [[1qe1\|1qe1]], [[1npa\|1npa]], [[1ajx\|1ajx]], [[1ebk\|1ebk]], [[1tvr\|1tvr]], [[1s6p\|1s6p]], [[1ikv\|1ikv]], [[1bqm\|1bqm]], [[1w5y\|1w5y]], [[1hos\|1hos]], [[1ikw\|1ikw]], [[1s6q\|1s6q]], [[3hvt\|3hvt]], [[1ec1\|1ec1]], [[1ec0\|1ec0]], [[2xyf\|2xyf]], [[1t05\|1t05]], [[1rvq\|1rvq]], [[1d4i\|1d4i]], [[1meu\|1meu]], [[1s9g\|1s9g]], [[2be2\|2be2]], [[1hnv\|1hnv]], [[1rvr\|1rvr]], [[1ikx\|1ikx]], [[1w5w\|1w5w]], [[1iky\|1iky]], [[1qmc\|1qmc]], [[1n6q\|1n6q]], [[1d4h\|1d4h]], [[1rvn\|1rvn]], [[1hbv\|1hbv]], [[1htf\|1htf]], [[1rtd\|1rtd]], [[1ec2\|1ec2]], [[2hmi\|2hmi]], [[1w5v\|1w5v]], [[1sv5\|1sv5]], [[2uy0\|2uy0]], [[1hmv\|1hmv]], [[2bbb\|2bbb]], [[1s9e\|1s9e]], [[2x4u\|2x4u]], [[1n5y\|1n5y]], [[1dlo\|1dlo]], [[1heg\|1heg]], [[1rvp\|1rvp]], [[1rvl\|1rvl]], [[1dw6\|1dw6]], [[1eet\|1eet]], [[1w5x\|1w5x]], [[1yt9\|1yt9]], [[2b6a\|2b6a]], [[1htg\|1htg]], [[1hvu\|1hvu]], [[1ebw\|1ebw]], [[2ban\|2ban]], [[1rdh\|1rdh]], [[2xye\|2xye]], [[1eby\|1eby]], [[1j5o\|1j5o]], [[1rvo\|1rvo]], [[1hvp\|1hvp]], [[1mes\|1mes]], [[1ec3\|1ec3]], [[1hef\|1hef]], [[1hih\|1hih]], [[1hni\|1hni]], [[1tv6\|1tv6]], [[1a9m\|1a9m]], [[1ebz\|1ebz]], [[2b5j\|2b5j]], [[1hys\|1hys]], [[1met\|1met]], [[1t03\|1t03]], [[1axa\|1axa]], [[1mer\|1mer]], [[1npw\|1npw]], [[3tlh\|3tlh]], [[1suq\|1suq]], [[2uxz\|2uxz]], [[1hvk\|1hvk]], [[1sbg\|1sbg]], [[1bqn\|1bqn]], [[1uwb\|1uwb]], [[2vg5\|2vg5]], [[1rvm\|1rvm]], [[1hte\|1hte]], [[1hrh\|1hrh]], [[1npv\|1npv]], [[1hqu\|1hqu]], [[2ykm\|2ykm]]</td></tr>
-	<tr~~><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class~~='~~plainlinks~~'~~>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [http://www.ebi.ac.uk/pdbsum/2ykn PDBsum]</span></td></tr>
-	~~<tr~~><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [http://www.ebi.ac.uk/pdbsum/2ykn PDBsum]</span></td></tr>	+	</table>
-	<table>	+	== Function ==
		+	[[http://www.uniprot.org/uniprot/POL_HV1B1 POL_HV1B1]] Gag-Pol polyprotein and Gag polyprotein may regulate their own translation, by the binding genomic RNA in the 5'-UTR. At low concentration, Gag-Pol and Gag would promote translation, whereas at high concentration, the polyproteins encapsidate genomic RNA and then shutt off translation (By similarity).<ref>PMID:9658129</ref> Matrix protein p17 has two main functions: in infected cell, it targets Gag and Gag-pol polyproteins to the plasma membrane via a multipartite membrane-binding signal, that includes its myristoylated N-terminus. The second function is to play a role in nuclear localization of the viral genome at the very start of cell infection. Matrix protein is the part of the pre-integration complex. It binds in the cytoplasm the human BAF protein which prevent autointegration of the viral genome, and might be included in virions at the ration of zero to 3 BAF dimer per virion. The myristoylation signal and the NLS thus exert conflicting influences its subcellular localization. The key regulation of these motifs might be phosphorylation of a portion of MA molecules on the C-terminal tyrosine at the time of virus maturation, by virion-associated cellular tyrosine kinase. Implicated in the release from host cell mediated by Vpu (By similarity).<ref>PMID:9658129</ref> Capsid protein p24 forms the conical core that encapsulates the genomic RNA-nucleocapsid complex in the virion. Most core are conical, with only 7% tubular. The core is constituted by capsid protein hexamer subunits. The core is disassembled soon after virion entry. Interaction with human PPIA/CYPA protects the virus from restriction by human TRIM5-alpha and from an unknown antiviral activity in human cells. This capsid restriction by TRIM5 is one of the factors which restricts HIV-1 to the human species (By similarity).<ref>PMID:9658129</ref> Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers. Facilitates rearangement of nucleic acid secondary structure during retrotranscription of genomic RNA. This capability is referred to as nucleic acid chaperone activity (By similarity).<ref>PMID:9658129</ref> The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell. Also cleaves Nef and Vif, probably concomitantly with viral structural proteins on maturation of virus particles (By similarity).<ref>PMID:9658129</ref> Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that converts the viral RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA(3)-Lys binds to the primer-binding site (PBS) situated at the 5'-end of the viral RNA. RT uses the 3' end of the tRNA primer to perform a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perform the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for two polypurine tracts (PPTs) situated at the 5'-end and near the center of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPTs that have not been removed by RNase H as primers. PPTs and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends (By similarity).<ref>PMID:9658129</ref> Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein, Vpr and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step, the PIC enters cell nucleus. This process is mediated through integrase and Vpr proteins, and allows the virus to infect a non dividing cell. This ability to enter the nucleus is specific of lentiviruses, other retroviruses cannot and rely on cell division to access cell chromosomes. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The 5'-ends are produced by integrase-catalyzed staggered cuts, 5 bp apart. A Y-shaped, gapped, recombination intermediate results, with the 5'-ends of the viral DNA strands and the 3' ends of target DNA strands remaining unjoined, flanking a gap of 5 bp. The last step is viral DNA integration into host chromosome. This involves host DNA repair synthesis in which the 5 bp gaps between the unjoined strands are filled in and then ligated. Since this process occurs at both cuts flanking the HIV genome, a 5 bp duplication of host DNA is produced at the ends of HIV-1 integration. Alternatively, Integrase may catalyze the excision of viral DNA just after strand transfer, this is termed disintegration (By similarity).<ref>PMID:9658129</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 14:		Line 15:
	Difluoromethylbenzoxazole Pyrimidine Thioether Derivatives: A Novel Class of Potent Non-Nucleoside HIV-1 Reverse Transcriptase Inhibitors.,Boyer J, Arnoult E, Medebielle M, Guillemont J, Unge J, Jochmans D J Med Chem. 2011 Dec 8;54(23):7974-85. Epub 2011 Nov 4. PMID:22017513<ref>PMID:22017513</ref>		Difluoromethylbenzoxazole Pyrimidine Thioether Derivatives: A Novel Class of Potent Non-Nucleoside HIV-1 Reverse Transcriptase Inhibitors.,Boyer J, Arnoult E, Medebielle M, Guillemont J, Unge J, Jochmans D J Med Chem. 2011 Dec 8;54(23):7974-85. Epub 2011 Nov 4. PMID:22017513<ref>PMID:22017513</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, a database of the U.S. National Library of Medicine.<br>	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
	== References ==		== References ==
Line 21:		Line 22:
	</StructureSection>		</StructureSection>
	[[Category: Human immunodeficiency virus type 1 bh10]]		[[Category: Human immunodeficiency virus type 1 bh10]]
-	[[Category: Arnoult, E.]]	+	[[Category: Arnoult, E]]
-	[[Category: Boyer, J.]]	+	[[Category: Boyer, J]]
-	[[Category: Guillemont, J.]]	+	[[Category: Guillemont, J]]
-	[[Category: Jochmans, D.]]	+	[[Category: Jochmans, D]]
-	[[Category: Medebielle, M.]]	+	[[Category: Medebielle, M]]
-	[[Category: Unge, J.]]	+	[[Category: Unge, J]]
-	[[Category: Unge, T.]]	+	[[Category: Unge, T]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 07:51, 14 May 2014

OCA — Wed, 14 May 2014 07:51:10 GMT

←Older revision		Revision as of 07:51, 14 May 2014
Line 1:		Line 1:
-	[[~~Image:~~2ykn.~~png~~\|~~left~~\|~~200px~~]]	+	==CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) IN COMPLEX WITH A DIFLUOROMETHYLBENZOXAZOLE (DFMB) PYRIMIDINE THIOETHER DERIVATIVE, A NON-NUCLEOSIDE RT INHIBITOR (NNRTI)==
		+	<StructureSection load='2ykn' size='340' side='right' caption='[[2ykn]], [[Resolution\|resolution]] 2.12Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_bh10 Human immunodeficiency virus type 1 bh10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=YKN:2-[DIFLUORO-[(4-METHYL-PYRIMIDINYL)-THIO]METHYL]-BENZOXAZOLE'>YKN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vg7\|2vg7]], [[1ajv\|1ajv]], [[1har\|1har]], [[1hps\|1hps]], [[1t7k\|1t7k]], [[1d4j\|1d4j]], [[1r0a\|1r0a]], [[1hpz\|1hpz]], [[2vg6\|2vg6]], [[1hqe\|1hqe]], [[1qe1\|1qe1]], [[1npa\|1npa]], [[1ajx\|1ajx]], [[1ebk\|1ebk]], [[1tvr\|1tvr]], [[1s6p\|1s6p]], [[1ikv\|1ikv]], [[1bqm\|1bqm]], [[1w5y\|1w5y]], [[1hos\|1hos]], [[1ikw\|1ikw]], [[1s6q\|1s6q]], [[3hvt\|3hvt]], [[1ec1\|1ec1]], [[1ec0\|1ec0]], [[2xyf\|2xyf]], [[1t05\|1t05]], [[1rvq\|1rvq]], [[1d4i\|1d4i]], [[1meu\|1meu]], [[1s9g\|1s9g]], [[2be2\|2be2]], [[1hnv\|1hnv]], [[1rvr\|1rvr]], [[1ikx\|1ikx]], [[1w5w\|1w5w]], [[1iky\|1iky]], [[1qmc\|1qmc]], [[1n6q\|1n6q]], [[1d4h\|1d4h]], [[1rvn\|1rvn]], [[1hbv\|1hbv]], [[1htf\|1htf]], [[1rtd\|1rtd]], [[1ec2\|1ec2]], [[2hmi\|2hmi]], [[1w5v\|1w5v]], [[1sv5\|1sv5]], [[2uy0\|2uy0]], [[1hmv\|1hmv]], [[2bbb\|2bbb]], [[1s9e\|1s9e]], [[2x4u\|2x4u]], [[1n5y\|1n5y]], [[1dlo\|1dlo]], [[1heg\|1heg]], [[1rvp\|1rvp]], [[1rvl\|1rvl]], [[1dw6\|1dw6]], [[1eet\|1eet]], [[1w5x\|1w5x]], [[1yt9\|1yt9]], [[2b6a\|2b6a]], [[1htg\|1htg]], [[1hvu\|1hvu]], [[1ebw\|1ebw]], [[2ban\|2ban]], [[1rdh\|1rdh]], [[2xye\|2xye]], [[1eby\|1eby]], [[1j5o\|1j5o]], [[1rvo\|1rvo]], [[1hvp\|1hvp]], [[1mes\|1mes]], [[1ec3\|1ec3]], [[1hef\|1hef]], [[1hih\|1hih]], [[1hni\|1hni]], [[1tv6\|1tv6]], [[1a9m\|1a9m]], [[1ebz\|1ebz]], [[2b5j\|2b5j]], [[1hys\|1hys]], [[1met\|1met]], [[1t03\|1t03]], [[1axa\|1axa]], [[1mer\|1mer]], [[1npw\|1npw]], [[3tlh\|3tlh]], [[1suq\|1suq]], [[2uxz\|2uxz]], [[1hvk\|1hvk]], [[1sbg\|1sbg]], [[1bqn\|1bqn]], [[1uwb\|1uwb]], [[2vg5\|2vg5]], [[1rvm\|1rvm]], [[1hte\|1hte]], [[1hrh\|1hrh]], [[1npv\|1npv]], [[1hqu\|1hqu]], [[2ykm\|2ykm]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ykn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ykn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ykn RCSB], [http://www.ebi.ac.uk/pdbsum/2ykn PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	This paper reports the synthesis and antiviral properties of new difluoromethylbenzoxazole (DFMB) pyrimidine thioether derivatives as non-nucleoside HIV-1 reverse transcriptase inhibitors. By use of a combination of structural biology study and traditional medicinal chemistry, several members of this novel class were synthesized using a single electron transfer chain process (radical nucleophilic substitution, S(RN)1) and were found to be potent against wild-type HIV-1 reverse transcriptase, with low cytotoxicity but with moderate activity against drug-resistant strains. The most promising compound 24 showed a significant EC(50) value close to 6.4 nM against HIV-1 IIIB, a moderate EC(50) value close to 54 muM against an NNRTI resistant double mutant (K103N + Y181C), but an excellent selectivity index >15477 (CC(50) > 100 muM).

-	<!--	+	Difluoromethylbenzoxazole Pyrimidine Thioether Derivatives: A Novel Class of Potent Non-Nucleoside HIV-1 Reverse Transcriptase Inhibitors.,Boyer J, Arnoult E, Medebielle M, Guillemont J, Unge J, Jochmans D J Med Chem. 2011 Dec 8;54(23):7974-85. Epub 2011 Nov 4. PMID:22017513<ref>PMID:22017513</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_2ykn"~~, ~~creates the "Structure Box" on the page~~.	+
-	~~You may change the PDB parameter~~ (~~which sets the PDB file loaded into the applet~~)	+
-	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~	+
-	~~or leave the SCENE parameter empty for the default display.~~	+
-	-->	+
-	~~{{STRUCTURE_2ykn\| PDB=2ykn \| SCENE= }}~~	+

-	~~===CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) IN COMPLEX WITH A DIFLUOROMETHYLBENZOXAZOLE (DFMB) PYRIMIDINE THIOETHER DERIVATIVE~~, ~~A NON-NUCLEOSIDE RT INHIBITOR (NNRTI)===~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_22017513}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 22017513 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_22017513}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2ykn]] is a 2 chain structure with sequence from [http:~~//en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_bh10 Human immunodeficiency virus type 1 bh10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA].	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:022017513<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Human immunodeficiency virus type 1 bh10]]		[[Category: Human immunodeficiency virus type 1 bh10]]
	[[Category: Arnoult, E.]]		[[Category: Arnoult, E.]]

OCA at 10:49, 14 December 2011

OCA — Wed, 14 Dec 2011 10:49:53 GMT

←Older revision		Revision as of 10:49, 14 December 2011
Line 1:		Line 1:
-	[[Image:2ykn.~~jpg~~\|left\|200px]]	+	[[Image:2ykn.png\|left\|200px]]

	<!--		<!--
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	===CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) IN COMPLEX WITH A DIFLUOROMETHYLBENZOXAZOLE (DFMB) PYRIMIDINE THIOETHER DERIVATIVE, A NON-NUCLEOSIDE RT INHIBITOR (NNRTI)===		===CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) IN COMPLEX WITH A DIFLUOROMETHYLBENZOXAZOLE (DFMB) PYRIMIDINE THIOETHER DERIVATIVE, A NON-NUCLEOSIDE RT INHIBITOR (NNRTI)===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22017513}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22017513 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22017513}}

	==About this Structure==		==About this Structure==
	[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_bh10 Human immunodeficiency virus type 1 bh10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA].		[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_bh10 Human immunodeficiency virus type 1 bh10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022017513</ref><references group="xtra"/>
	[[Category: Human immunodeficiency virus type 1 bh10]]		[[Category: Human immunodeficiency virus type 1 bh10]]
	[[Category: Arnoult, E.]]		[[Category: Arnoult, E.]]

OCA at 06:23, 17 August 2011

OCA — Wed, 17 Aug 2011 06:23:51 GMT

←Older revision		Revision as of 06:23, 17 August 2011
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:2ykn.jpg\|left\|200px]]

-	The ~~entry 2ykn~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_2ykn", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_2ykn\| PDB=2ykn \| SCENE= }}

-	~~Authors: Boyer~~, ~~J., Arnoult, E., Medebielle, M., Guillemont, J., Unge, T., Unge, J., Jochmans, D.~~	+	===CRYSTAL STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) IN COMPLEX WITH A DIFLUOROMETHYLBENZOXAZOLE (DFMB) PYRIMIDINE THIOETHER DERIVATIVE, A NON-NUCLEOSIDE RT INHIBITOR (NNRTI)===

-	~~Description: Crystal~~ structure ~~of HIV~~-1 ~~Reverse Transcriptase (RT) in complex with a Difluoromethylbenzoxazole (DFMB) Pyrimidine Thioether derivative~~, ~~a non-nucleoside RT inhibitor (NNRTI)~~	+
		+	==About this Structure==
		+	[[2ykn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_bh10 Human immunodeficiency virus type 1 bh10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YKN OCA].
		+	[[Category: Human immunodeficiency virus type 1 bh10]]
		+	[[Category: Arnoult, E.]]
		+	[[Category: Boyer, J.]]
		+	[[Category: Guillemont, J.]]
		+	[[Category: Jochmans, D.]]
		+	[[Category: Medebielle, M.]]
		+	[[Category: Unge, J.]]
		+	[[Category: Unge, T.]]
		+	[[Category: Hydrolase]]