Caspase-3/Sandbox: Difference between revisions
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{{STRUCTURE_1qx3 | PDB=1qx3 | SCENE=Caspase-3/Sandbox/Unliganded_human_caspase-3/4 | CAPTION= Crystal Structure of Unliganded Human Caspase-3}} | {{STRUCTURE_1qx3 | PDB=1qx3 | SCENE=Caspase-3/Sandbox/Unliganded_human_caspase-3/4 | CAPTION= Crystal Structure of Unliganded Human Caspase-3}} | ||
Caspases are proteases that function via a cysteine residue in the active site to cleave substrates after aspartic acid residues. Caspases are crucial for the initiation (e.g. caspase-8, -9, -10) and execution (e.g. caspase-3, -6, -7) of apoptosis, or programmed cell death either via the intrinsic or extrinsic pathway (Degterev, Boyce et al. 2003). In its inactive form, '''procaspase-3''' consist of a large subunit and small subunit, interjected by an aspartic acid residue. This aspartate is the site recognized by activated initiator caspases, such as caspase-8 and caspase-9. Upon cleavage, procaspase-3 is separated into two subunits, p17/20 and p12/10 respectively, which heterodimerize to yield the active form of '''caspase-3'''. In its active form, caspase-3 is able to cleave substrates such as ICAD (inhibitor of caspase-activated deoxyribonuclease). Cleavage of ICAD leads to abrogation of its inhibitory effect on CAD, allowing CAD to migrate into the nucleus and cause double-strand breaks in DNA, thus contributing to apoptosis(Enari, Sakahira et al. 1998; Sakahira, Enari et al. 1998). | '''Caspases''' are proteases that function via a cysteine residue in the active site to cleave substrates after aspartic acid residues. Caspases are crucial for the initiation (e.g. caspase-8, -9, -10) and execution (e.g. caspase-3, -6, -7) of apoptosis, or programmed cell death either via the intrinsic or extrinsic pathway (Degterev, Boyce et al. 2003). In its inactive form, '''procaspase-3''' consist of a large subunit and small subunit, interjected by an aspartic acid residue. This aspartate is the site recognized by activated initiator caspases, such as caspase-8 and caspase-9. Upon cleavage, procaspase-3 is separated into two subunits, p17/20 and p12/10 respectively, which heterodimerize to yield the active form of '''caspase-3'''. In its active form, caspase-3 is able to cleave substrates such as ICAD (inhibitor of caspase-activated deoxyribonuclease). Cleavage of ICAD leads to abrogation of its inhibitory effect on CAD, allowing CAD to migrate into the nucleus and cause double-strand breaks in DNA, thus contributing to apoptosis(Enari, Sakahira et al. 1998; Sakahira, Enari et al. 1998). | ||
==Structure & Function== | ==Structure & Function== | ||