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Caspase-3 Structure
Caspases are synthesized in the cell in their zymogen forms, consisting of an N-terminal prodomain followed by a large and a small subunit linked to each other by an intersubunit linker. As an executioner caspase, caspase-3 has a short N-terminal prodomain and like any other caspases, cleavage of the intersubunit linker at a specific aspartate residue generates the mature form of the enzyme. Caspase-3 in its functional form is dimeric, with the dimer interface being stabilized by interactions between the small subunits of each monomer. Binding of a , such as DEVD-CHO to the active site of the enzyme induces a conformational change that allows the L2 and L2' loops to interlock and stabilize the active site .
