3od5: Difference between revisions
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==Crystal structure of active caspase-6 bound with Ac-VEID-CHO== | ==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=''> | <StructureSection load='3od5' size='340' side='right'caption='[[3od5]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3od5]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3od5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3nr2|3nr2]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Caspase-6 Caspase-6], with EC number [https://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'>[ | <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> | </table> | ||
== Function == | == 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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 23: | ||
==See Also== | ==See Also== | ||
*[[Caspase|Caspase]] | *[[Caspase 3D structures|Caspase 3D structures]] | ||
*[[Caspase-6 and neurodegeneration|Caspase-6 and neurodegeneration]] | *[[Caspase-6 and neurodegeneration|Caspase-6 and neurodegeneration]] | ||
*[[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]] | ||
| Line 34: | Line 33: | ||
[[Category: Caspase-6]] | [[Category: Caspase-6]] | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Cao, Q]] | [[Category: Cao, Q]] | ||
[[Category: Liu, X]] | [[Category: Liu, X]] | ||
Revision as of 13:40, 18 May 2022
Crystal structure of active caspase-6 bound with Ac-VEID-CHOCrystal structure of active caspase-6 bound with Ac-VEID-CHO
Structural highlights
Function[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. 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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