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The | ==HIV-1 protease (D25N, inactive) in complex with phage display optimized substrate SGIFLETS== | ||
<StructureSection load='6bra' size='340' side='right'caption='[[6bra]], [[Resolution|resolution]] 1.11Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6bra]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_fd Enterobacteria phage fd] and [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=6BRA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BRA FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.111Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=6bra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bra OCA], [https://pdbe.org/6bra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bra RCSB], [https://www.ebi.ac.uk/pdbsum/6bra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bra ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5RZ08_9HIV1 Q5RZ08_9HIV1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Crystal structures of inactive variants of HIV-1 protease bound to peptides have revealed how the enzyme recognizes its endogenous substrates. The best of the known substrates is, however, a nonnatural substrate that was identified by directed evolution. The crystal structure of the complex between this substrate and the D25N variant of the protease is reported at a resolution of 1.1 A. The structure has several unprecedented features, especially the formation of additional hydrogen bonds between the enzyme and the substrate. This work expands the understanding of molecular recognition by HIV-1 protease and informs the design of new substrates and inhibitors. | |||
A substrate selected by phage display exhibits enhanced side-chain hydrogen bonding to HIV-1 protease.,Windsor IW, Raines RT Acta Crystallogr D Struct Biol. 2018 Jul 1;74(Pt 7):690-694. doi:, 10.1107/S2059798318006691. Epub 2018 Jun 27. PMID:29968678<ref>PMID:29968678</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6bra" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Immunodeficiency virus protease 3D structures|Immunodeficiency virus protease 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Enterobacteria phage fd]] | |||
[[Category: Human immunodeficiency virus 1]] | |||
[[Category: Large Structures]] | |||
[[Category: Raines RT]] | |||
[[Category: Windsor IW]] | |||
Latest revision as of 17:48, 4 October 2023
HIV-1 protease (D25N, inactive) in complex with phage display optimized substrate SGIFLETSHIV-1 protease (D25N, inactive) in complex with phage display optimized substrate SGIFLETS
Structural highlights
FunctionPublication Abstract from PubMedCrystal structures of inactive variants of HIV-1 protease bound to peptides have revealed how the enzyme recognizes its endogenous substrates. The best of the known substrates is, however, a nonnatural substrate that was identified by directed evolution. The crystal structure of the complex between this substrate and the D25N variant of the protease is reported at a resolution of 1.1 A. The structure has several unprecedented features, especially the formation of additional hydrogen bonds between the enzyme and the substrate. This work expands the understanding of molecular recognition by HIV-1 protease and informs the design of new substrates and inhibitors. A substrate selected by phage display exhibits enhanced side-chain hydrogen bonding to HIV-1 protease.,Windsor IW, Raines RT Acta Crystallogr D Struct Biol. 2018 Jul 1;74(Pt 7):690-694. doi:, 10.1107/S2059798318006691. Epub 2018 Jun 27. PMID:29968678[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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