Caspase
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
<StructureSection load='1pyo' size='350' side='right' scene='45/458455/Cv/1' caption='CASP-2 subunit P18 (purple, yellow) and subunit P12 (green, cyan) complex with polypeptide inhibitor (salmon, blue), aspartic aldehyde and acetyl group, [[1pyo]]'> | <StructureSection load='1pyo' size='350' side='right' scene='45/458455/Cv/1' caption='CASP-2 subunit P18 (purple, 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 (see [[Protease]]) 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 /> |
* '''CASP-1''' (or '''Interleukin-1 beta converting enzyme, ICE''') cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein. See [[Human Caspase-1]]<br /> | * '''CASP-1''' (or '''Interleukin-1 beta converting enzyme, ICE''') cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein. See [[Human Caspase-1]]<br /> | ||
* '''CASP-3''' or ('''Apopain; Cysteine protease CPP32''') interacts with CASP-8 and CASP-9 during cell apoptosis. See [[Sandox Bay Serrano]], [[Student Projects for UMass Chemistry 423 Spring 2012-5]] and [[Caspase-3 Regulatory Mechanisms]]<br /> | * '''CASP-3''' or ('''Apopain; Cysteine protease CPP32''') interacts with CASP-8 and CASP-9 during cell apoptosis. See [[Sandox Bay Serrano]], [[Student Projects for UMass Chemistry 423 Spring 2012-5]] and [[Caspase-3 Regulatory Mechanisms]]<br /> |
Revision as of 10:07, 4 February 2019
|
3D structures of caspase
Updated on 04-February-2019
4jqy, 4jqz - hpro-CASP (mutant)
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