3od5: 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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3OD5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ASA:ASPARTIC+ALDEHYDE'>ASA</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene></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=3od5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3od5 OCA], [https://pdbe.org/3od5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3od5 RCSB], [https://www.ebi.ac.uk/pdbsum/3od5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3od5 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CASP6_HUMAN CASP6_HUMAN] Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death. | |||
<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> | |||
<div class="pdbe-citations 3od5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Caspase 3D structures|Caspase 3D structures]] | |||
*[[Caspase-6 and neurodegeneration|Caspase-6 and neurodegeneration]] | |||
*[[Molecular Playground/Caspase-6 and neurodegeneration|Molecular Playground/Caspase-6 and neurodegeneration]] | |||
*[[User:Kevin Buadlart Dagbay|User:Kevin Buadlart Dagbay]] | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Cao | [[Category: Large Structures]] | ||
[[Category: Liu | [[Category: Cao Q]] | ||
[[Category: Su | [[Category: Liu X]] | ||
[[Category: Wang | [[Category: Su X-D]] | ||
[[Category: Wang | [[Category: Wang K-T]] | ||
[[Category: Wang X-J]] | |||
Latest revision as of 19:54, 1 November 2023
Crystal structure of active caspase-6 bound with Ac-VEID-CHOCrystal structure of active caspase-6 bound with Ac-VEID-CHO
Structural highlights
FunctionCASP6_HUMAN Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death. Publication Abstract from PubMedDimeric 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also
References
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