5d63: Difference between revisions
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CF0:FLUOROMETHANE'>CF0</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CF0:FLUOROMETHANE'>CF0</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ef2|3ef2]], [[2iho|2iho]], [[5d61|5d61]], [[5d62|5d62]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ef2|3ef2]], [[2iho|2iho]], [[5d61|5d61]], [[5d62|5d62]]</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=5d63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d63 OCA], [http://pdbe.org/5d63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d63 RCSB], [http://www.ebi.ac.uk/pdbsum/5d63 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=5d63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d63 OCA], [http://pdbe.org/5d63 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d63 RCSB], [http://www.ebi.ac.uk/pdbsum/5d63 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d63 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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Revision as of 17:20, 22 December 2016
MOA-Z-VAD-fmk inhibitor complex, direct/inverted dual orientationMOA-Z-VAD-fmk inhibitor complex, direct/inverted dual orientation
Structural highlights
Publication Abstract from PubMedPapain-like cysteine proteases (PLCPs) constitute the largest group of thiol-based protein degrading enzymes and are characterized by a highly conserved fold. They are found in bacteria, viruses, plants and animals and involved in a number of physiological and pathological processes, parasitic infections and host defense, making them interesting targets for drug design. The Marasmius oreades agglutinin (MOA) is a blood group B-specific fungal chimerolectin with calcium-dependent proteolytic activity. The proteolytic domain of MOA presents a unique structural arrangement, yet mimicking the main structural elements in known PLCPs. Here we present the X-ray crystal structure of MOA in complex with Z-VAD-fmk, an irreversible caspase inhibitor known to cross-react with PLCPs. The structural data allow modeling of the substrate binding geometry and mapping of the fundamental enzyme-substrate interactions. The new information consolidates MOA as a new, yet strongly atypical member of the papain superfamily. The reported complex is the first published structure of a PLCP in complex with the well characterized caspase inhibitor Z-VAD-fmk. An Unusual Member of the Papain Superfamily: Mapping the Catalytic Cleft of the Marasmius oreades agglutinin (MOA) with a Caspase Inhibitor.,Cordara G, van Eerde A, Grahn EM, Winter HC, Goldstein IJ, Krengel U PLoS One. 2016 Feb 22;11(2):e0149407. doi: 10.1371/journal.pone.0149407., eCollection 2016. PMID:26901797[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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