4dqg - Revision history

OCA at 08:34, 21 September 2022

OCA — Wed, 21 Sep 2022 08:34:25 GMT

←Older revision		Revision as of 08:34, 21 September 2022
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	==Crystal Structure of apo(G16C/L38C) HIV-1 Protease==		==Crystal Structure of apo(G16C/L38C) HIV-1 Protease==
-	<StructureSection load='4dqg' size='340' side='right' caption='[[4dqg]], [[Resolution\|resolution]] 2.79Å' scene=''>	+	<StructureSection load='4dqg' size='340' side='right'caption='[[4dqg]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4dqg]] 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=4DQG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4DQG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4dqg]] 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=4DQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DQG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HGU:N-HYDROXYGUANIDINE'>HGU</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HGU:N-HYDROXYGUANIDINE'>HGU</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dqb\|4dqb]], [[4dqc\|4dqc]], [[4dqe\|4dqe]], [[4dqf\|4dqf]], [[4dqh\|4dqh]]</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=4dqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dqg OCA], [https://pdbe.org/4dqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dqg RCSB], [https://www.ebi.ac.uk/pdbsum/4dqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dqg ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">gag-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1])~~</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=4dqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dqg OCA], [~~http~~://pdbe.org/4dqg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4dqg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4dqg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4dqg ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[[https://www.uniprot.org/uniprot/POL_HV1Z2 POL_HV1Z2]] 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;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 4dqg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4dqg" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Immunodeficiency virus protease 3D structures\|Immunodeficiency virus protease 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Mittal, S~~]]	+	[[Category: Human immunodeficiency virus 1]]
-	[[Category: ~~Schiffer, C A~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Aid~~]]	+	[[Category: Mittal S]]
-	[[Category: ~~Drug design]]~~	+	[[Category: Schiffer CA]]
-	~~[[Category: Drug resistance]]~~	+
-	~~[[Category: Hiv-1 protease]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Protease inhibitor~~]]	+

OCA at 07:56, 15 November 2017

OCA — Wed, 15 Nov 2017 07:56:23 GMT

←Older revision		Revision as of 07:56, 15 November 2017
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	</div>		</div>
	<div class="pdbe-citations 4dqg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4dqg" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Virus protease\|Virus protease]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:35, 11 December 2016

OCA — Sun, 11 Dec 2016 02:35:59 GMT

←Older revision		Revision as of 02:35, 11 December 2016
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		+
	==Crystal Structure of apo(G16C/L38C) HIV-1 Protease==		==Crystal Structure of apo(G16C/L38C) HIV-1 Protease==
	<StructureSection load='4dqg' size='340' side='right' caption='[[4dqg]], [[Resolution\|resolution]] 2.79Å' scene=''>		<StructureSection load='4dqg' size='340' side='right' caption='[[4dqg]], [[Resolution\|resolution]] 2.79Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4dqg]] is a 2 chain structure with sequence from [http://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=4DQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DQG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4dqg]] 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=4DQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DQG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HGU:N-HYDROXYGUANIDINE'>HGU</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HGU:N-HYDROXYGUANIDINE'>HGU</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dqb\|4dqb]], [[4dqc\|4dqc]], [[4dqe\|4dqe]], [[4dqf\|4dqf]], [[4dqh\|4dqh]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dqb\|4dqb]], [[4dqc\|4dqc]], [[4dqe\|4dqe]], [[4dqf\|4dqf]], [[4dqh\|4dqh]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">gag-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 ~~Human immunodeficiency virus 1~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">gag-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 9HIV1])</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=4dqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dqg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dqg RCSB], [http://www.ebi.ac.uk/pdbsum/4dqg 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=4dqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dqg OCA], [http://pdbe.org/4dqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dqg RCSB], [http://www.ebi.ac.uk/pdbsum/4dqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dqg ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	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 4dqg" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 23:		Line 25:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Human immunodeficiency virus 1]]
	[[Category: Mittal, S]]		[[Category: Mittal, S]]
	[[Category: Schiffer, C A]]		[[Category: Schiffer, C A]]

OCA at 17:08, 9 December 2014

OCA — Tue, 09 Dec 2014 17:08:58 GMT

←Older revision		Revision as of 17:08, 9 December 2014
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-	[[~~Image:~~4dqg.~~png~~\|~~left~~\|~~200px~~]]	+	==Crystal Structure of apo(G16C/L38C) HIV-1 Protease==
		+	<StructureSection load='4dqg' size='340' side='right' caption='[[4dqg]], [[Resolution\|resolution]] 2.79Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4dqg]] is a 2 chain structure with sequence from [http://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=4DQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DQG FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HGU:N-HYDROXYGUANIDINE'>HGU</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4dqb\|4dqb]], [[4dqc\|4dqc]], [[4dqe\|4dqe]], [[4dqf\|4dqf]], [[4dqh\|4dqh]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">gag-pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1])</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=4dqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dqg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dqg RCSB], [http://www.ebi.ac.uk/pdbsum/4dqg PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Human immunodeficiency virus Type-1 (HIV-1) protease is crucial for viral maturation and infectivity. Studies of protease dynamics suggest that the rearrangement of the hydrophobic core is essential for enzyme activity. Many mutations in the hydrophobic core are also associated with drug resistance and may modulate the core flexibility. To test the role of flexibility in protease activity, pairs of cysteines were introduced at the interfaces of flexible regions remote from the active site. Disulfide bond formation was confirmed by crystal structures and by alkylation of free cysteines and mass spectrometry. Oxidized and reduced crystal structures of these variants show the overall structure of the protease is retained. However, cross-linking the cysteines led to drastic loss in enzyme activity, which was regained upon reducing the disulfide cross-links. Molecular dynamics simulations showed that altered dynamics propagated throughout the enzyme from the engineered disulfide. Thus, altered flexibility within the hydrophobic core can modulate HIV-1 protease activity, supporting the hypothesis that drug resistant mutations distal from the active site can alter the balance between substrate turnover and inhibitor binding by modulating enzyme activity.

-	~~{{STRUCTURE_4dqg\| PDB=4dqg \| SCENE= }}~~	+	Hydrophobic Core Flexibility Modulates Enzyme Activity in HIV-1 Protease.,Mittal S, Cai Y, Nalam MN, Bolon DN, Schiffer CA J Am Chem Soc. 2012 Mar 7;134(9):4163-8. Epub 2012 Feb 28. PMID:22295904<ref>PMID:22295904</ref>

-	~~===Crystal Structure of apo(G16C~~/~~L38C) HIV-1 Protease===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_22295904}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[4dqg]] is~~ a ~~2 chain structure with sequence from [http://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=4DQG OCA].~~	+

	==See Also==		==See Also==
	*[[Virus protease\|Virus protease]]		*[[Virus protease\|Virus protease]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:022295904<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Human immunodeficiency virus 1]]		[[Category: Human immunodeficiency virus 1]]
-	[[Category: Mittal, S.]]	+	[[Category: Mittal, S]]
-	[[Category: Schiffer, C A.]]	+	[[Category: Schiffer, C A]]
	[[Category: Aid]]		[[Category: Aid]]
	[[Category: Drug design]]		[[Category: Drug design]]

OCA at 16:55, 20 October 2012

OCA — Sat, 20 Oct 2012 16:55:28 GMT

←Older revision		Revision as of 16:55, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[4dqg]] is a 2 chain structure ~~of [[Virus protease]]~~ with sequence from [http://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=4DQG OCA].	+	[[4dqg]] is a 2 chain structure with sequence from [http://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=4DQG OCA].

	==See Also==		==See Also==

OCA at 23:15, 26 July 2012

OCA — Thu, 26 Jul 2012 23:15:21 GMT

←Older revision		Revision as of 23:15, 26 July 2012
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	[[Image:4dqg.png\|left\|200px]]		[[Image:4dqg.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_4dqg\| PDB=4dqg \| SCENE= }}		{{STRUCTURE_4dqg\| PDB=4dqg \| SCENE= }}

	===Crystal Structure of apo(G16C/L38C) HIV-1 Protease===		===Crystal Structure of apo(G16C/L38C) HIV-1 Protease===

-
-	<!--
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	{{ABSTRACT_PUBMED_22295904}}		{{ABSTRACT_PUBMED_22295904}}

	==About this Structure==		==About this Structure==
-	[[4dqg]] is a 2 chain structure with sequence from [http://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=4DQG OCA].	+	[[4dqg]] is a 2 chain structure of [[Virus protease]] with sequence from [http://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=4DQG OCA].
		+
		+	==See Also==
		+	*[[Virus protease\|Virus protease]]

	==Reference==		==Reference==

OCA at 18:13, 2 May 2012

OCA — Wed, 02 May 2012 18:13:22 GMT

←Older revision		Revision as of 18:13, 2 May 2012
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-	[[Image:4dqg.~~jpg~~\|left\|200px]]	+	[[Image:4dqg.png\|left\|200px]]

	<!--		<!--

OCA at 05:43, 8 March 2012

OCA — Thu, 08 Mar 2012 05:43:02 GMT

←Older revision		Revision as of 05:43, 8 March 2012
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-	~~'''Unreleased structure'''~~	+	[[Image:4dqg.jpg\|left\|200px]]

-	The ~~entry 4dqg~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_4dqg", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
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		+	or leave the SCENE parameter empty for the default display.
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		+	{{STRUCTURE_4dqg\| PDB=4dqg \| SCENE= }}

-	~~Authors: Schiffer, C.A., Mittal, S.~~	+	===Crystal Structure of apo(G16C/L38C) HIV-1 Protease===

-	~~Description: Crystal Structure of apo~~(~~G16C~~/~~L38C~~) ~~HIV~~-1 Protease	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22295904}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22295904 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22295904}}
		+
		+	==About this Structure==
		+	[[4dqg]] is a 2 chain structure with sequence from [http://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=4DQG OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022295904</ref><references group="xtra"/>
		+	[[Category: Human immunodeficiency virus 1]]
		+	[[Category: Mittal, S.]]
		+	[[Category: Schiffer, C A.]]
		+	[[Category: Aid]]
		+	[[Category: Drug design]]
		+	[[Category: Drug resistance]]
		+	[[Category: Hiv-1 protease]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Protease inhibitor]]

OCA at 08:24, 29 February 2012

OCA — Wed, 29 Feb 2012 08:24:26 GMT

←Older revision		Revision as of 08:24, 29 February 2012
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4dqg is ON HOLD	+	The entry 4dqg is ON HOLD until Paper Publication

	Authors: Schiffer, C.A., Mittal, S.		Authors: Schiffer, C.A., Mittal, S.

	Description: Crystal Structure of apo(G16C/L38C) HIV-1 Protease		Description: Crystal Structure of apo(G16C/L38C) HIV-1 Protease

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

OCA — Wed, 22 Feb 2012 07:33:07 GMT

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

←Older revision

Revision as of 07:33, 22 February 2012