User:Daniel Seeman/DELETE

spinqualitylabelsall models Toggle between active site inhibitor bound and allosterically inhibited caspase-7 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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.

Forms of Caspase-7

• Caspase-7 bound to dead-end substrate mimic DEVD-CHO, trapping protein in active/substrate bound conformation.
• Caspase-7 bound to allosteric inhibitor DICA through CYS290 trapping protein in a form incompatible with substrate binding.
• Conformational change between substrate bound and substrate incompatible forms of Caspase-7.

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Molecular Playground banner: Conformational Dynamics between active and allosterically inhibited caspase-7 elucidate the mechanism of allostery in this important class of cysteine proteases.

Proteopedia Page Contributors and Editors (what is this?)

Daniel Seeman, Jaime Prilusky