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4qj2

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Crystal structure of inactive HIV-1 protease variant (I50V/A71V) in complex with WT p1-p6 substrate

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Retrieved from "http://52.214.119.220/wiki/index.php/4qj2"

Categories: Human immunodeficiency virus 1 | Large Structures | Lin KH | Schiffer CA

@@ Line 3: / Line 3: @@
 <StructureSection load='4qj2' size='340' side='right'caption='[[4qj2]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4qj2]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QJ2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QJ2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4qj2]] is a 6 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=4QJ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QJ2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.13&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qj6|4qj6]], [[4qj7|4qj7]], [[4qj8|4qj8]], [[4qj9|4qj9]], [[4qja|4qja]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4qj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qj2 OCA], [http://pdbe.org/4qj2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qj2 RCSB], [http://www.ebi.ac.uk/pdbsum/4qj2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qj2 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=4qj2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qj2 OCA], [https://pdbe.org/4qj2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qj2 RCSB], [https://www.ebi.ac.uk/pdbsum/4qj2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qj2 ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/O38710_9HIV1 O38710_9HIV1]
-Drug resistance mutations in response to HIV-1 protease inhibitors are selected not only in the drug target but elsewhere in the viral genome, especially at the protease cleavage sites in the precursor protein Gag. To understand the molecular basis of this protease-substrate coevolution, we solved the crystal structures of drug resistant I50V/A71V HIV-1 protease with p1-p6 substrates bearing coevolved mutations. Analyses of the protease-substrate interactions reveal that compensatory coevolved mutations in the substrate do not restore interactions lost due to protease mutations, but instead establish other interactions that are not restricted to the site of mutation. Mutation of a substrate residue has distal effects on other residues' interactions as well, including through the induction of a conformational change in the protease. Additionally, molecular dynamics simulations suggest that restoration of active site dynamics is an additional constraint in the selection of coevolved mutations. Hence, protease-substrate coevolution permits mutational, structural, and dynamic changes via molecular mechanisms that involve distal effects contributing to drug resistance.
-Structural basis and distal effects of Gag substrate coevolution in drug resistance to HIV-1 protease.,Ozen A, Lin KH, Kurt Yilmaz N, Schiffer CA Proc Natl Acad Sci U S A. 2014 Nov 11;111(45):15993-8. doi:, 10.1073/pnas.1414063111. Epub 2014 Oct 29. PMID:25355911<ref>PMID:25355911</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4qj2" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Immunodeficiency virus protease 3D structures|Immunodeficiency virus protease 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Human immunodeficiency virus 1]]
 [[Category: Large Structures]]
-[[Category: Lin, K H]]
+[[Category: Lin KH]]
-[[Category: Schiffer, C A]]
+[[Category: Schiffer CA]]
-[[Category: Co-evolution]]
-[[Category: Hydrolase]]
-[[Category: Protease]]

4qj2

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Current revision

Crystal structure of inactive HIV-1 protease variant (I50V/A71V) in complex with WT p1-p6 substrate

Structural highlights

Function

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