User:Daniel Seeman/DELETE: Difference between revisions
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Conformational dynamics in Caspase-7 are mediated by an 'Allosteric Toggle' mechanism in which binding of allosteric inhibitor DICA is bound to CYS 290 and pushes TYR 223 into 'up' conformation forcing ARG 187 'out' into a form that is physically incompatible with substrate binding. | Conformational dynamics in Caspase-7 are mediated by an 'Allosteric Toggle' mechanism in which binding of allosteric inhibitor DICA is bound to CYS 290 and pushes TYR 223 into 'up' conformation forcing ARG 187 'out' into a form that is physically incompatible with substrate binding. | ||
The cleaved termini of the large and small subunits which form the active site loop bundle become highly ordered in active site conformation, and highly disordered in allosterically inhibited form. | The cleaved termini of the large and small subunits which form the active site loop bundle become highly ordered in active site conformation, and highly disordered in allosterically inhibited form (so much so that they cannot be resolved crystallographically). | ||
=== Forms of Caspase-7 === | === Forms of Caspase-7 === | ||
