Caspase
From Proteopedia
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| - | <StructureSection load='1pyo' size='450' side='right' scene='' caption='CASP-2 subunit P18 (grey, pink) and subunit P12 (green, yellow) complex with polypeptide inhibitor (magenta, cyan), aspartic aldehyde and acetyl group, [[1pyo]]'> | + | <StructureSection load='1pyo' size='450' side='right' scene='45/458455/Cv/1' caption='CASP-2 subunit P18 (grey, pink) and subunit P12 (green, yellow) complex with polypeptide inhibitor (magenta, cyan), aspartic aldehyde and acetyl group, [[1pyo]]'> |
'''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.<br /> | '''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.<br /> | ||
Revision as of 09:29, 22 November 2015
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3D structures of caspase
Updated on 22-November-2015
