Sandox Bay Serrano

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 <scene name='Sandox_Bay_Serrano/Scene01_substrate/2'>substrate</scene>, 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 <scene name='Sandox_Bay_Serrano/Scene01_substrate/3'>TextToBeDisplayed</scene>.