Caspase

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Revision as of 10:43, 24 July 2011 by Michal Harel (talk | contribs) (New page: {{STRUCTURE_3d6f| PDB=3d6f | SIZE=300| SCENE= |right| CAPTION=CASP-1 complex with polypeptide inhibitor, 3d6f }} '''Caspase''' (CASP) are cysteine-aspartic proteases which funct...)
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Template:STRUCTURE 3d6f

Caspase (CASP) are cysteine-aspartic proteases which function in apoptosis, necrosis and inflammation. Twelve CASP have been identified in human. CASP is synthesized as an inactive pro-CASP with a prodomain which is being cleaved off to render them active. The X-linked inhibitor of apoptosis protein (XIAP) with its baculoviral IAP repeat (BIR) domain is an inhibitor of CASP. CASP-1 cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein. CASP-3 interacts with CASP-8 and CASP-9 during cell apoptosis.


3D structures of factor IX3D structures of factor IX

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Michal Harel, Alexander Berchansky