User:Daniel Seeman/DELETE: Difference between revisions
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Forms of Caspase-7
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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' /> | <applet load='Caspmorph.pdb' size='300' frame='true' align='right' caption='Toggle between active site inhibitor bound and allosterically inhibited caspase-7' /> | ||
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 === | === Forms of Caspase-7 === | ||
Revision as of 19:03, 3 May 2010
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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-7Forms of Caspase-7
- , trapping protein in active/substrate bound conformation.
- trapping protein in a form incompatible with substrate binding.
- 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.