3od5
From Proteopedia
(Difference between revisions)
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- | + | ==Crystal structure of active caspase-6 bound with Ac-VEID-CHO== | |
- | + | <StructureSection load='3od5' size='340' side='right' caption='[[3od5]], [[Resolution|resolution]] 1.60Å' scene=''> | |
- | + | == Structural highlights == | |
+ | <table><tr><td colspan='2'>[[3od5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OD5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OD5 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene></td></tr> | ||
+ | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ASA:ASPARTIC+ALDEHYDE'>ASA</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nr2|3nr2]]</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-6 Caspase-6], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.59 3.4.22.59] </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=3od5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3od5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3od5 RCSB], [http://www.ebi.ac.uk/pdbsum/3od5 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Dimeric effectors caspase 3 and caspase 7 are activated by initiator caspase processing. In this study, we report the crystal structures of effector caspase 6 (CASP6) zymogen and N-Acetyl-Val-Glu-Ile-Asp-al-inhibited CASP6. Both of these forms of CASP6 have a dimeric structure, and in CASP6 zymogen the intersubunit cleavage site (190)TEVD(193) is well structured and inserts into the active site. This positions residue Asp 193 to be easily attacked by the catalytic residue Cys 163. We demonstrate biochemically that intramolecular cleavage at Asp 193 is a prerequisite for CASP6 self-activation and that this activation mechanism is dependent on the length of the L2 loop. Our results indicate that CASP6 can be activated and regulated through intramolecular self-cleavage. | ||
- | + | Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation.,Wang XJ, Cao Q, Liu X, Wang KT, Mi W, Zhang Y, Li LF, Leblanc AC, Su XD EMBO Rep. 2010 Oct 1. PMID:20890311<ref>PMID:20890311</ref> | |
- | + | ||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
==See Also== | ==See Also== | ||
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*[[Molecular Playground/Caspase-6 and neurodegeneration|Molecular Playground/Caspase-6 and neurodegeneration]] | *[[Molecular Playground/Caspase-6 and neurodegeneration|Molecular Playground/Caspase-6 and neurodegeneration]] | ||
*[[User:Kevin Buadlart Dagbay|User:Kevin Buadlart Dagbay]] | *[[User:Kevin Buadlart Dagbay|User:Kevin Buadlart Dagbay]] | ||
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
+ | </StructureSection> | ||
[[Category: Caspase-6]] | [[Category: Caspase-6]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Cao, Q | + | [[Category: Cao, Q]] |
- | [[Category: Liu, X | + | [[Category: Liu, X]] |
- | [[Category: Su, X D | + | [[Category: Su, X D]] |
- | [[Category: Wang, K T | + | [[Category: Wang, K T]] |
- | [[Category: Wang, X J | + | [[Category: Wang, X J]] |
[[Category: Apoptotic protease]] | [[Category: Apoptotic protease]] | ||
[[Category: Caspase domain]] | [[Category: Caspase domain]] | ||
[[Category: Hydrolase-hydrolase inhibitor complex]] | [[Category: Hydrolase-hydrolase inhibitor complex]] |
Revision as of 08:32, 18 December 2014
Crystal structure of active caspase-6 bound with Ac-VEID-CHO
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