3sm1: Difference between revisions
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<StructureSection load='3sm1' size='340' side='right'caption='[[3sm1]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='3sm1' size='340' side='right'caption='[[3sm1]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3sm1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3sm1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/DG-75_Murine_leukemia_virus DG-75 Murine leukemia virus] and [https://en.wikipedia.org/wiki/Streptomyces_argenteolus_subsp._toyonakensis Streptomyces argenteolus subsp. toyonakensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SM1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=IVA:ISOVALERIC+ACID'>IVA</scene>, <scene name='pdbligand=STA:STATINE'>STA</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=3sm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sm1 OCA], [https://pdbe.org/3sm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sm1 RCSB], [https://www.ebi.ac.uk/pdbsum/3sm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sm1 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=3sm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sm1 OCA], [https://pdbe.org/3sm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sm1 RCSB], [https://www.ebi.ac.uk/pdbsum/3sm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sm1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9E7M1_9GAMR Q9E7M1_9GAMR] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: DG-75 Murine leukemia virus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptomyces argenteolus subsp. toyonakensis]] | ||
[[Category: | [[Category: Gustchina A]] | ||
[[Category: Li M]] | |||
[[Category: | [[Category: Wlodawer A]] | ||
[[Category: | |||
Latest revision as of 13:26, 6 November 2024
The crystal structure of XMRV protease complexed with pepstatin AThe crystal structure of XMRV protease complexed with pepstatin A
Structural highlights
FunctionPublication Abstract from PubMedInteractions between the protease (PR) encoded by the xenotropic murine leukemia virus-related virus and a number of potential inhibitors have been investigated by biochemical and structural techniques. It was observed that several inhibitors used clinically against HIV PR exhibit nanomolar or even subnanomolar values of K(i) , depending on the exact experimental conditions. Both TL-3, a universal inhibitor of retroviral PRs, and some inhibitors originally shown to inhibit plasmepsins were also quite potent, whereas inhibition by pepstatin A was considerably weaker. Crystal structures of the complexes of xenotropic murine leukemia virus-related virus PR with TL-3, amprenavir and pepstatin A were solved at high resolution and compared with the structures of complexes of these inhibitors with other retropepsins. Whereas TL-3 and amprenavir bound in a predictable manner, spanning the substrate-binding site of the enzyme, two molecules of pepstatin A bound simultaneously in an unprecedented manner, leaving the catalytic water molecule in place. Structured digital abstract * XMRVPR and XMRVPR bind by x-ray crystallography (View interaction). Structural and biochemical characterization of the inhibitor complexes of xenotropic murine leukemia virus-related virus protease.,Li M, Gustchina A, Matuz K, Tozser J, Namwong S, Goldfarb NE, Dunn BM, Wlodawer A FEBS J. 2011 Sep 23. doi: 10.1111/j.1742-4658.2011.08364.x. PMID:21951660[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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