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5wvc
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the CARD-CARD disk== | |
| + | <StructureSection load='5wvc' size='340' side='right' caption='[[5wvc]], [[Resolution|resolution]] 2.99Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5wvc]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WVC FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></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=5wvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wvc OCA], [http://pdbe.org/5wvc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wvc RCSB], [http://www.ebi.ac.uk/pdbsum/5wvc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wvc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/APAF_HUMAN APAF_HUMAN]] Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis.<ref>PMID:10393175</ref> <ref>PMID:12804598</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Death domain (DD)-fold assemblies play a crucial role in regulating the signaling to cell survival or death. Here we report the crystal structure of the caspase recruitment domain (CARD)-CARD disk of the human apoptosome. The structure surprisingly reveals that three 1:1 Apaf-1:procaspase-9 CARD protomers form a novel helical DD-fold assembly on the heptameric wheel-like platform of the apoptosome. The small-angle X-ray scattering and multi-angle light scattering data also support that three protomers could form an oligomeric complex similar to the crystal structure. Interestingly, the quasi-equivalent environment of CARDs could generate different quaternary CARD assemblies. We also found that the type II interaction is conserved in all DD-fold complexes, whereas the type I interaction is found only in the helical DD-fold assemblies. This study provides crucial insights into the caspase activation mechanism, which is tightly controlled by a sophisticated and highly evolved CARD assembly on the apoptosome, and also enables better understanding of the intricate DD-fold assembly. | ||
| - | + | Structural Insights into DD-Fold Assembly and Caspase-9 Activation by the Apaf-1 Apoptosome.,Su TW, Yang CY, Kao WP, Kuo BJ, Lin SM, Lin JY, Lo YC, Lin SC Structure. 2017 Mar 7;25(3):407-420. doi: 10.1016/j.str.2016.12.019. Epub 2017, Jan 19. PMID:28111022<ref>PMID:28111022</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Lo, Y | + | <div class="pdbe-citations 5wvc" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lin, S C]] | ||
| + | [[Category: Lo, Y C]] | ||
| + | [[Category: Su, T W]] | ||
| + | [[Category: Apoptosis]] | ||
| + | [[Category: Protein-protein interaction]] | ||
| + | [[Category: Signaling protein complex]] | ||
Revision as of 13:05, 19 April 2017
Structure of the CARD-CARD disk
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