4cf8 - Revision history

OCA at 12:09, 20 December 2023

2023-12-20T12:09:13Z

←Older revision		Revision as of 12:09, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CF8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CF8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V7H:(2S)-2-(3-HYDROXY-3-OXOPROPYL)-6-[[[2-[(PHENYLMETHYL)CARBAMOYL]PHENYL]METHYLAMINO]METHYL]-2,3-DIHYDRO-1,4-BENZODIOXINE-5-CARBOXYLIC+ACID'>V7H</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]] 1.65Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V7H:(2S)-2-(3-HYDROXY-3-OXOPROPYL)-6-[[[2-[(PHENYLMETHYL)CARBAMOYL]PHENYL]METHYLAMINO]METHYL]-2,3-DIHYDRO-1,4-BENZODIOXINE-5-CARBOXYLIC+ACID'>V7H</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=4cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf8 OCA], [https://pdbe.org/4cf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cf8 RCSB], [https://www.ebi.ac.uk/pdbsum/4cf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cf8 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=4cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf8 OCA], [https://pdbe.org/4cf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cf8 RCSB], [https://www.ebi.ac.uk/pdbsum/4cf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cf8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/POL_HV1N5 POL_HV1N5]] 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). 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). 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). 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). 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). 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). 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).	+	[https://www.uniprot.org/uniprot/POL_HV1N5 POL_HV1N5] 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). 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). 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). 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). 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). 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). 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).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Tremendous gains and novel methods are often developed when people are challenged to do something new or difficult. This process is enhanced when people compete against each other-this can be seen in sport as well as in science and technology (e.g. the space race). The SAMPL challenges, like the CASP challenges, aim to challenge modellers and software developers to develop new ways of looking at molecular interactions so the community as a whole can progress in the accurate prediction of these interactions. In order for this challenge to occur, data must be supplied so the prospective test can be done. We have supplied unpublished data related to a drug discovery program run several years ago on HIV integrase for the SAMPL4 challenge. This paper describes the methods used to obtain these data and the chemistry involved.
		+
		+	Interrogating HIV integrase for compounds that bind- a SAMPL challenge.,Peat TS, Dolezal O, Newman J, Mobley D, Deadman JJ J Comput Aided Mol Des. 2014 Feb 16. PMID:24532034<ref>PMID:24532034</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4cf8" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:42, 7 September 2022

2022-09-07T17:42:41Z

←Older revision		Revision as of 17:42, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4cf8' size='340' side='right'caption='[[4cf8]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='4cf8' size='340' side='right'caption='[[4cf8]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4cf8]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~9hiv1 9hiv1~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4CF8 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4cf8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CF8 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V7H:(2S)-2-(3-HYDROXY-3-OXOPROPYL)-6-[[[2-[(PHENYLMETHYL)CARBAMOYL]PHENYL]METHYLAMINO]METHYL]-2,3-DIHYDRO-1,4-BENZODIOXINE-5-CARBOXYLIC+ACID'>V7H</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V7H:(2S)-2-(3-HYDROXY-3-OXOPROPYL)-6-[[[2-[(PHENYLMETHYL)CARBAMOYL]PHENYL]METHYLAMINO]METHYL]-2,3-DIHYDRO-1,4-BENZODIOXINE-5-CARBOXYLIC+ACID'>V7H</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ce9\|4ce9]], [[4cea\|4cea]], [[4ceb\|4ceb]], [[4cec\|4cec]], [[4ced\|4ced]], [[4cee\|4cee]], [[4cef\|4cef]], [[4ceo\|4ceo]], [[4ceq\|4ceq]], [[4cer\|4cer]], [[4ces\|4ces]], [[4cez\|4cez]], [[4cf0\|4cf0]], [[4cf1\|4cf1]], [[4cf2\|4cf2]], [[4cf9\|4cf9]], [[4cfa\|4cfa]], [[4cfb\|4cfb]], [[4cfc\|4cfc]], [[4cfd\|4cfd]]</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=4cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf8 OCA], [https://pdbe.org/4cf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cf8 RCSB], [https://www.ebi.ac.uk/pdbsum/4cf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cf8 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=4cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf8 OCA], [~~http~~://pdbe.org/4cf8 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4cf8 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4cf8 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4cf8 ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[[https://www.uniprot.org/uniprot/POL_HV1N5 POL_HV1N5]] 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). 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). 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). 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). 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). 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). 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).
-	~~Tremendous gains~~ and ~~novel methods are often developed when people are challenged~~ to ~~do something new or difficult~~. ~~This process~~ is ~~enhanced when people compete against each other~~-~~this can~~ be ~~seen~~ in ~~sport as well as in science~~ and ~~technology (e~~.g. the ~~space race~~). ~~The SAMPL challenges, like~~ the ~~CASP challenges~~, ~~aim~~ to ~~challenge modellers~~ and ~~software developers~~ to ~~develop new ways~~ of ~~looking at molecular interactions so~~ the ~~community~~ as a ~~whole~~ can ~~progress~~ in the ~~accurate prediction~~ of ~~these interactions~~. ~~In order for this challenge~~ to ~~occur~~, ~~data must be supplied so~~ the ~~prospective test~~ can be ~~done~~. We have ~~supplied unpublished data related~~ to a ~~drug discovery program run several years ago on HIV~~ integrase ~~for~~ the ~~SAMPL4 challenge~~. This ~~paper describes~~ the ~~methods used~~ to ~~obtain these data~~ and the ~~chemistry involved~~.	+
-		+
-	~~Interrogating HIV~~ integrase ~~for compounds that bind~~- ~~a SAMPL challenge~~.,~~Peat TS~~, ~~Dolezal O~~, ~~Newman J~~, ~~Mobley D, Deadman JJ J Comput Aided Mol Des~~. ~~2014 Feb 16~~. ~~PMID:24532034<ref>PMID:24532034</ref>~~	+
-		+
-	~~From MEDLINE®/PubMed®~~, a ~~database~~ of the U.~~S. National Library~~ of ~~Medicine~~.~~<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 4cf8" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~DNA-directed DNA polymerase~~]]	+	[[Category: Human immunodeficiency virus 1]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Peat~~, T S]]~~	+	[[Category: Peat TS]]
-	~~[[Category: Structure based drug design]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 09:29, 20 March 2019

2019-03-20T09:29:09Z

←Older revision		Revision as of 09:29, 20 March 2019
Line 1:		Line 1:

	==Interrogating HIV integrase for compounds that bind- a SAMPL challenge==		==Interrogating HIV integrase for compounds that bind- a SAMPL challenge==
-	<StructureSection load='4cf8' size='340' side='right' caption='[[4cf8]], [[Resolution\|resolution]] 1.65Å' scene=''>	+	<StructureSection load='4cf8' size='340' side='right'caption='[[4cf8]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CF8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CF8 FirstGlance]. <br>
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: DNA-directed DNA polymerase]]		[[Category: DNA-directed DNA polymerase]]
		+	[[Category: Large Structures]]
	[[Category: Peat, T S]]		[[Category: Peat, T S]]
	[[Category: Structure based drug design]]		[[Category: Structure based drug design]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 18:10, 11 August 2016

2016-08-11T18:10:52Z

←Older revision		Revision as of 18:10, 11 August 2016
Line 1:		Line 1:
		+
	==Interrogating HIV integrase for compounds that bind- a SAMPL challenge==		==Interrogating HIV integrase for compounds that bind- a SAMPL challenge==
	<StructureSection load='4cf8' size='340' side='right' caption='[[4cf8]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='4cf8' size='340' side='right' caption='[[4cf8]], [[Resolution\|resolution]] 1.65Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ce9\|4ce9]], [[4cea\|4cea]], [[4ceb\|4ceb]], [[4cec\|4cec]], [[4ced\|4ced]], [[4cee\|4cee]], [[4cef\|4cef]], [[4ceo\|4ceo]], [[4ceq\|4ceq]], [[4cer\|4cer]], [[4ces\|4ces]], [[4cez\|4cez]], [[4cf0\|4cf0]], [[4cf1\|4cf1]], [[4cf2\|4cf2]], [[4cf9\|4cf9]], [[4cfa\|4cfa]], [[4cfb\|4cfb]], [[4cfc\|4cfc]], [[4cfd\|4cfd]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ce9\|4ce9]], [[4cea\|4cea]], [[4ceb\|4ceb]], [[4cec\|4cec]], [[4ced\|4ced]], [[4cee\|4cee]], [[4cef\|4cef]], [[4ceo\|4ceo]], [[4ceq\|4ceq]], [[4cer\|4cer]], [[4ces\|4ces]], [[4cez\|4cez]], [[4cf0\|4cf0]], [[4cf1\|4cf1]], [[4cf2\|4cf2]], [[4cf9\|4cf9]], [[4cfa\|4cfa]], [[4cfb\|4cfb]], [[4cfc\|4cfc]], [[4cfd\|4cfd]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=4cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cf8 RCSB], [http://www.ebi.ac.uk/pdbsum/4cf8 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=4cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf8 OCA], [http://pdbe.org/4cf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cf8 RCSB], [http://www.ebi.ac.uk/pdbsum/4cf8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cf8 ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	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 4cf8" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:01, 4 January 2015

2015-01-04T13:01:41Z

←Older revision		Revision as of 13:01, 4 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4cf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CF8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4cf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CF8 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V7H:(2S)-2-(3-HYDROXY-3-OXOPROPYL)-6-[[[2-[(PHENYLMETHYL)CARBAMOYL]PHENYL]METHYLAMINO]METHYL]-2,3-DIHYDRO-1,4-BENZODIOXINE-5-CARBOXYLIC+ACID'>V7H</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V7H:(2S)-2-(3-HYDROXY-3-OXOPROPYL)-6-[[[2-[(PHENYLMETHYL)CARBAMOYL]PHENYL]METHYLAMINO]METHYL]-2,3-DIHYDRO-1,4-BENZODIOXINE-5-CARBOXYLIC+ACID'>V7H</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ce9\|4ce9]], [[4cea\|4cea]], [[4ceb\|4ceb]], [[4cec\|4cec]], [[4ced\|4ced]], [[4cee\|4cee]], [[4cef\|4cef]], [[4ceo\|4ceo]], [[4ceq\|4ceq]], [[4cer\|4cer]], [[4ces\|4ces]], [[4cez\|4cez]], [[4cf0\|4cf0]], [[4cf1\|4cf1]], [[4cf2\|4cf2]], [[4cf9\|4cf9]], [[4cfa\|4cfa]], [[4cfb\|4cfb]], [[4cfc\|4cfc]], [[4cfd\|4cfd]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ce9\|4ce9]], [[4cea\|4cea]], [[4ceb\|4ceb]], [[4cec\|4cec]], [[4ced\|4ced]], [[4cee\|4cee]], [[4cef\|4cef]], [[4ceo\|4ceo]], [[4ceq\|4ceq]], [[4cer\|4cer]], [[4ces\|4ces]], [[4cez\|4cez]], [[4cf0\|4cf0]], [[4cf1\|4cf1]], [[4cf2\|4cf2]], [[4cf9\|4cf9]], [[4cfa\|4cfa]], [[4cfb\|4cfb]], [[4cfc\|4cfc]], [[4cfd\|4cfd]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=4cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cf8 RCSB], [http://www.ebi.ac.uk/pdbsum/4cf8 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=4cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cf8 RCSB], [http://www.ebi.ac.uk/pdbsum/4cf8 PDBsum]</span></td></tr>
-	<table>	+	</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 20:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: 9hiv1]]
	[[Category: DNA-directed DNA polymerase]]		[[Category: DNA-directed DNA polymerase]]
-	[[Category: Peat, T S.]]	+	[[Category: Peat, T S]]
	[[Category: Structure based drug design]]		[[Category: Structure based drug design]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 05:14, 25 June 2014

2014-06-25T05:14:26Z

←Older revision		Revision as of 05:14, 25 June 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4cf8\| PDB=4cf8 \| SCENE= }}~~	+	==Interrogating HIV integrase for compounds that bind- a SAMPL challenge==
-	===Interrogating HIV integrase for compounds that bind- a SAMPL challenge===	+	<StructureSection load='4cf8' size='340' side='right' caption='[[4cf8]], [[Resolution\|resolution]] 1.65Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24532034}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4cf8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/9hiv1 9hiv1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CF8 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=V7H:(2S)-2-(3-HYDROXY-3-OXOPROPYL)-6-[[[2-[(PHENYLMETHYL)CARBAMOYL]PHENYL]METHYLAMINO]METHYL]-2,3-DIHYDRO-1,4-BENZODIOXINE-5-CARBOXYLIC+ACID'>V7H</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4ce9\|4ce9]], [[4cea\|4cea]], [[4ceb\|4ceb]], [[4cec\|4cec]], [[4ced\|4ced]], [[4cee\|4cee]], [[4cef\|4cef]], [[4ceo\|4ceo]], [[4ceq\|4ceq]], [[4cer\|4cer]], [[4ces\|4ces]], [[4cez\|4cez]], [[4cf0\|4cf0]], [[4cf1\|4cf1]], [[4cf2\|4cf2]], [[4cf9\|4cf9]], [[4cfa\|4cfa]], [[4cfb\|4cfb]], [[4cfc\|4cfc]], [[4cfd\|4cfd]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=4cf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cf8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4cf8 RCSB], [http://www.ebi.ac.uk/pdbsum/4cf8 PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Tremendous gains and novel methods are often developed when people are challenged to do something new or difficult. This process is enhanced when people compete against each other-this can be seen in sport as well as in science and technology (e.g. the space race). The SAMPL challenges, like the CASP challenges, aim to challenge modellers and software developers to develop new ways of looking at molecular interactions so the community as a whole can progress in the accurate prediction of these interactions. In order for this challenge to occur, data must be supplied so the prospective test can be done. We have supplied unpublished data related to a drug discovery program run several years ago on HIV integrase for the SAMPL4 challenge. This paper describes the methods used to obtain these data and the chemistry involved.

-	~~==About this Structure==~~	+	Interrogating HIV integrase for compounds that bind- a SAMPL challenge.,Peat TS, Dolezal O, Newman J, Mobley D, Deadman JJ J Comput Aided Mol Des. 2014 Feb 16. PMID:24532034<ref>PMID:24532034</ref>
-	~~[[4cf8]] is~~ a ~~2 chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4CF8 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024532034</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: 9hiv1]]
	[[Category: DNA-directed DNA polymerase]]		[[Category: DNA-directed DNA polymerase]]
	[[Category: Peat, T S.]]		[[Category: Peat, T S.]]
	[[Category: Structure based drug design]]		[[Category: Structure based drug design]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 14:34, 3 March 2014

2014-03-03T14:34:44Z

←Older revision		Revision as of 14:34, 3 March 2014
Line 1:		Line 1:
	{{STRUCTURE_4cf8\| PDB=4cf8 \| SCENE= }}		{{STRUCTURE_4cf8\| PDB=4cf8 \| SCENE= }}
	===Interrogating HIV integrase for compounds that bind- a SAMPL challenge===		===Interrogating HIV integrase for compounds that bind- a SAMPL challenge===
		+	{{ABSTRACT_PUBMED_24532034}}

	==About this Structure==		==About this Structure==
	[[4cf8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA].		[[4cf8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:024532034</ref><references group="xtra"/><references/>
	[[Category: DNA-directed DNA polymerase]]		[[Category: DNA-directed DNA polymerase]]
	[[Category: Peat, T S.]]		[[Category: Peat, T S.]]
	[[Category: Structure based drug design]]		[[Category: Structure based drug design]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 13:45, 11 December 2013

2013-12-11T13:45:46Z

←Older revision		Revision as of 13:45, 11 December 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4cf8\| PDB=4cf8 \| SCENE= }}
		+	===Interrogating HIV integrase for compounds that bind- a SAMPL challenge===

-	~~The entry~~ 4cf8 is ~~ON HOLD until sometime in the future~~	+	==About this Structure==
-		+	[[4cf8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CF8 OCA].
-	~~Authors~~: ~~PEAT~~, T.S.	+	[[Category: DNA-directed DNA polymerase]]
-		+	[[Category: Peat, T S.]]
-	~~Description~~: ~~Interrogating HIV integrase for compounds that bind-a SAMPL challenge~~	+	[[Category: Structure based drug design]]
		+	[[Category: Transferase]]

OCA at 06:31, 4 December 2013

2013-12-04T06:31:17Z

←Older revision		Revision as of 06:31, 4 December 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4cf8 is ON HOLD	+	The entry 4cf8 is ON HOLD until sometime in the future

	Authors: PEAT, T.S.		Authors: PEAT, T.S.

	Description: Interrogating HIV integrase for compounds that bind-a SAMPL challenge		Description: Interrogating HIV integrase for compounds that bind-a SAMPL challenge

OCA: Protected "4cf8" [edit=sysop:move=sysop]

2013-11-20T12:38:16Z

Protected "4cf8" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:38, 20 November 2013