Caspase: Difference between revisions

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Michal Harel, Alexander Berchansky

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	<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]]'>		<StructureSection load='1pyo' size='450' side='right' scene='45/458455/Cv/1' caption='CASP-2 subunit P18 (deeppink, yellow) and subunit P12 (green, cyan) complex with polypeptide inhibitor (salmon, blue), 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 />