User:Daniel Seeman/DELETE: Difference between revisions

Latest revision as of 13:35, 23 May 2018

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-<applet load='Caspmorph.pdb' size='300' frame='true' align='right' caption='Toggle between active site inhibitor bound and allosterically inhibited caspase-7' />
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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 pushing ARG 187 'out' into a form that is physically incompatible with substrate binding.
-=== Forms of Caspase-7 ===
-*<scene name='User:Daniel_Seeman/Caspase-7_Dynamics/1f1j/1'>Caspase-7 bound to dead-end substrate mimic DEVD-CHO</scene>, trapping protein in active/substrate bound conformation.
-*<scene name='User:Daniel_Seeman/Caspase-7_Dynamics/1shj-234234/1'>Caspase-7 bound to allosteric inhibitor DICA through CYS290</scene> trapping protein in a form incompatible with substrate binding.
-*<scene name='User:Daniel_Seeman/Caspase-7_Dynamics/Morph1/1'>Conformational change between substrate bound and substrate incompatible forms</scene> of Caspase-7.
-=== Molecular Playground banner ===
-'''Molecular Playground banner:''' Conformational Dynamics between active and allosterically inhibited caspase-7 elucidate the mechanism of allostery in this important class of cysteine proteases.