3qnw
From Proteopedia
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== 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. | [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 == | ||
| + | Caspase-6 is a cysteine protease implicated in neuronal survival and apoptosis. Deregulation of caspase-6 activity was linked to several neurodegenerative disorders including Alzheimer's and Huntington's Diseases. Several recent studies on the structure of caspase-6 feature the caspase-6 zymogen, mature apo-caspase-6 as well as the Ac-VEID-CHO peptide complex. All structures share the same typical dimeric caspase conformation. However, mature apo-caspase-6 crystallized at low pH revealed a novel, non-canonical inactive caspase conformation speculated to represent a latent state of the enzyme suitable for the design of allosteric inhibitors. In this treatise we present the structure of caspase-6 in the non-canonical inactive enzyme conformation bound to the irreversible inhibitor Z-VAD-FMK. The complex features a unique peptide binding mode not observed previously. | ||
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| + | Structure of human caspase-6 in complex with Z-VAD-FMK: New peptide binding mode observed for the non-canonical caspase conformation.,Muller I, Lamers MB, Ritchie AJ, Dominguez C, Munoz-Sanjuan I, Kiselyov A Bioorg Med Chem Lett. 2011 Sep 15;21(18):5244-7. Epub 2011 Jul 21. PMID:21820899<ref>PMID:21820899</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3qnw" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Caspase 3D structures|Caspase 3D structures]] | *[[Caspase 3D structures|Caspase 3D structures]] | ||
*[[Caspase-6 and neurodegeneration|Caspase-6 and neurodegeneration]] | *[[Caspase-6 and neurodegeneration|Caspase-6 and neurodegeneration]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Caspase-6 in complex with Z-VAD-FMK inhibitor
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Categories: Homo sapiens | Large Structures | Synthetic construct | Dominguez C | Kiselyov A | Lamers M | Maillard M | Mueller I | Munoz I | Park H | Ritchie A
