Caspase: Difference between revisions
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* '''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 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-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- | * '''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 /> | ||
[[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 /> | ||
* '''CASP-9''' is an aspartic protease linked to mitochondrial death pathway. See [[Molecular Playground/Caspase-9 Regulation]].<br /> | * '''CASP-9''' is an aspartic protease linked to mitochondrial death pathway. See [[Molecular Playground/Caspase-9 Regulation]].<br /> | ||
* '''Metacaspase''' (MCASP) are arginine/lysine specific CASP. MCASP are found in plants and fungi. | * '''Metacaspase''' (MCASP) are arginine/lysine specific CASP. MCASP are found in plants and fungi. | ||
==3D structures of caspase== | ==3D structures of caspase== | ||
Revision as of 14:54, 19 November 2015
Template:STRUCTURE 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.
- 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
- 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
- CASP-6 is involved in the activation of cascade of caspases during apoptosis. See Molecular Playground/Caspase-6 (new) and Caspase-6 and neurodegeneration
- 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
- CASP-9 is an aspartic protease linked to mitochondrial death pathway. See Molecular Playground/Caspase-9 Regulation.
- Metacaspase (MCASP) are arginine/lysine specific CASP. MCASP are found in plants and fungi.
3D structures of caspase3D structures of caspase
Updated on 19-November-2015