3sm2: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3sm2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Viruses Viruses]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SM2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3sm2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Viruses Viruses]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SM2 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nr6|3nr6]], [[3slz|3slz]], [[3sm1|3sm1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nr6|3nr6]], [[3slz|3slz]], [[3sm1|3sm1]]</td></tr> | ||
<tr><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=10239 Viruses])</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=10239 Viruses])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sm2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sm2 RCSB], [http://www.ebi.ac.uk/pdbsum/3sm2 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=3sm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sm2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sm2 RCSB], [http://www.ebi.ac.uk/pdbsum/3sm2 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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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> | 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 | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Viruses]] | [[Category: Viruses]] | ||
[[Category: Gustchina, A | [[Category: Gustchina, A]] | ||
[[Category: Li, M | [[Category: Li, M]] | ||
[[Category: Wlodawer, A | [[Category: Wlodawer, A]] | ||
[[Category: Amprenavir]] | [[Category: Amprenavir]] | ||
[[Category: Beta-sheet]] | [[Category: Beta-sheet]] | ||
Revision as of 13:58, 4 January 2015
Structural highlights
Publication 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. References
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