Caspase

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. 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, Student Projects for UMass Chemistry 423 Spring 2012-5 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 caspase Caspase 3D structures

spinqualitylabelsall models CASP-2 subunit P18 (purple, yellow) and subunit P12 (green, cyan) complex with polypeptide inhibitor (salmon, blue), aspartic aldehyde and acetyl group, 1pyo Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image