User:Daniel Seeman/DELETE: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
<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 | 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 === | === Forms of Caspase-7 === | ||
Revision as of 16:03, 3 May 2010
|
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.
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.
