View source for 3sm2


==The crystal structure of XMRV protease complexed with Amprenavir==
<StructureSection load='3sm2' size='340' side='right'caption='[[3sm2]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sm2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dg-75_murine_leukemia_virus Dg-75 murine leukemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SM2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=478:{3-[(4-AMINO-BENZENESULFONYL)-ISOBUTYL-AMINO]-1-BENZYL-2-HYDROXY-PROPYL}-CARBAMIC+ACID+TETRAHYDRO-FURAN-3-YL+ESTER'>478</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3nr6|3nr6]], [[3slz|3slz]], [[3sm1|3sm1]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag-pol ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=114654 DG-75 Murine leukemia virus])</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=3sm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sm2 OCA], [https://pdbe.org/3sm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sm2 RCSB], [https://www.ebi.ac.uk/pdbsum/3sm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sm2 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Interactions 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<ref>PMID:21951660</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3sm2" style="background-color:#fffaf0;"></div>

==See Also==
*[[Virus protease 3D structures|Virus protease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dg-75 murine leukemia virus]]
[[Category: Large Structures]]
[[Category: Gustchina, A]]
[[Category: Li, M]]
[[Category: Wlodawer, A]]
[[Category: Amprenavir]]
[[Category: Beta-sheet]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Protease]]
[[Category: Virus]]