Caspase: Difference between revisions

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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 '''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]] 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 />
*  '''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 />
*  '''CASP-7''' is a heterodimer consisting of P20 (human residues 1-198) and P11 (human residues 199-303) subunits.  CASP-7 catalytic domain consists of residues 57-303. is an important initiator CASP and drICE is an effector of apoptosis CASP in ''Drosophila melanogaster''.  See [[Molecular Playground/Caspase-7 Dynamics]] and [[Molecular Playground/Executioner Caspase-7]]<br />
*  '''CASP-7''' is a heterodimer consisting of P20 (human residues 1-198) and P11 (human residues 199-303) subunits.  CASP-7 catalytic domain consists of residues 57-303. is an important initiator CASP and drICE is an effector of apoptosis CASP in ''Drosophila melanogaster''.  See [[Molecular Playground/Caspase-7 Dynamics]] and [[Molecular Playground/Executioner Caspase-7]]<br />

Revision as of 11:18, 22 February 2016

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

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3D structures of caspase

Updated on 22-February-2016

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky