Caspase-3/Sandbox: Difference between revisions
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When cleaved into its active form, caspase-3 is then able to bind to its substrates via recognition of DEVD consensus sequence. Caspase-3, using its active site cysteine residue, is then able to cleave the substrate at the Asp residue occupying the P4 portion of the active site. This is a <scene name='Caspase-3/Sandbox/1qx3_2cjxv2_zdevdcmk/1'>morph</scene>([[1qx3]] to [[2cjx]])showing the binding of modified DEVD substrate (zDEVD-cmk) to the active site of caspase-3. | When cleaved into its active form, caspase-3 is then able to bind to its substrates via recognition of DEVD consensus sequence. Caspase-3, using its active site cysteine residue, is then able to cleave the substrate at the Asp residue occupying the P4 portion of the active site. This is a <scene name='Caspase-3/Sandbox/1qx3_2cjxv2_zdevdcmk/1'>morph</scene>([[1qx3]] to [[2cjx]])showing the binding of modified DEVD substrate (zDEVD-cmk) to the active site of caspase-3. | ||
[[Image:1pau devd inhibition3.png|420px|right|thumb| Inhibitor DEVD-CHO bound to Caspase-3, [[1PAU]]]] | |||
</StructureSection> | </StructureSection> | ||
===Function=== | ===Function=== | ||
(Structural insights into its function) | (Structural insights into its function) | ||
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, p18/20 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. | 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, p18/20 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). | ||
[[Image:ICAD | [[Image:ICAD.png|300px]] | ||
==Disease== | ==Disease== | ||