Caspase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <StructureSection load='1pyo' size='450' side='right' scene='45/458455/Cv/1' caption='CASP-2 subunit P18 ( | + | <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 /> | ||
Revision as of 09:23, 24 November 2015
| |||||||||||
3D structures of caspase
Updated on 24-November-2015
References
- ↑ Schweizer A, Briand C, Grutter MG. Crystal structure of caspase-2, apical initiator of the intrinsic apoptotic pathway. J Biol Chem. 2003 Oct 24;278(43):42441-7. Epub 2003 Aug 14. PMID:12920126 doi:http://dx.doi.org/10.1074/jbc.M304895200
- ↑ Wilson KP, Black JA, Thomson JA, Kim EE, Griffith JP, Navia MA, Murcko MA, Chambers SP, Aldape RA, Raybuck SA, et al.. Structure and mechanism of interleukin-1 beta converting enzyme. Nature. 1994 Jul 28;370(6487):270-5. PMID:8035875 doi:http://dx.doi.org/10.1038/370270a0
