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'''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 />
*  '''CASP-1''' (or I'''nterleukin-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]] 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]] and [[Caspase-3 Regulatory Mechanisms]]<br />
*  '''CASP-6''' is involved in the activation of cascade of caspases during apoptosis.  See [[Molecular Playground/Caspase-6 (new)]] and [[Caspase-6 and neurodegeneration]]<br />
*  '''CASP-6''' is involved in the activation of cascade of caspases during apoptosis.  See [[Molecular Playground/Caspase-6 (new)]] and [[Caspase-6 and neurodegeneration]]<br />

Revision as of 11:53, 6 December 2015


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.

[1][2]

CASP-2 subunit P18 (purple, yellow) and subunit P12 (green, cyan) complex with polypeptide inhibitor (salmon, blue), aspartic aldehyde and acetyl group, 1pyo

Drag the structure with the mouse to rotate

3D structures of caspase3D structures of caspase

Updated on 06-December-2015

ReferencesReferences

  1. ↑ 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
  2. ↑ 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

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