Caspase
From Proteopedia
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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.<br /> | * '''CASP-1''' (or I'''nterleukin-1 beta converting enzyme, ICE''') cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein.<br /> | ||
| - | * '''CASP-3''' interacts with CASP-8 and CASP-9 during cell apoptosis.<br /> | + | * '''CASP-3''' or ('''Apopain; Cysteine protease CPP32''') interacts with CASP-8 and CASP-9 during cell apoptosis.<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''.<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''.<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. | ||
Revision as of 09:50, 26 July 2015
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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.
- CASP-1 (or Interleukin-1 beta converting enzyme, ICE) cleaves precursor cytokine interleukin 1-β and interleukin 18 into mature protein.
- CASP-3 or (Apopain; Cysteine protease CPP32) interacts with CASP-8 and CASP-9 during cell apoptosis.
- 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.
- Metacaspase (MCASP) are arginine/lysine specific CASP. MCASP are found in plants and fungi.
For some details see:
CASP-1 - Human Caspase-1
CASP-3 - Sandox Bay Serrano;
CASP-6 - Molecular Playground/Caspase-6 (new);
CASP-7 - Molecular Playground/Caspase-7 Dynamics
CASP-9 - Molecular Playground/Caspase-9 Regulation.
3D structures of caspase
Updated on 26-July-2015
