User:Daniel Seeman/DELETE: Difference between revisions

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=== Conformation Dynamics studied in <span class="plainlinks">[http://www.chem.umass.edu/~jhardy/ the Hardy Lab] </span>===

Conformational dynamics in Caspase-7 are mediated by an 'Allosteric Toggle' mechanism in which binding of allosteric inhibitor DICA to CYS 290 pushes TYR 223 into 'up' conformation forcing ARG 187 'out' into a form that is physically incompatible with substrate binding.

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*<scene name='Molecular_Playground/Caspase_Dynamics/1f1j/2'>Caspase-7 bound to suicide inhibitor/substrate mimic DEVD-CHO</scene>, trapping protein in active/substrate bound conformation.

*<scene name='Molecular_Playground/Caspase_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='Molecular_Playground/Caspase_Dynamics/Morph2/1'>Conformational change between substrate bound and substrate incompatible forms</scene> of Caspase-7.

*<scene name='Molecular_Playground/Caspase_Dynamics/Morph2/2'>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.

@@ Line 2: / Line 2: @@
 === Conformation Dynamics studied in <span class="plainlinks">[http://www.chem.umass.edu/~jhardy/ the Hardy Lab] </span>===
-<applet load='Caspmorph.pdb' size='300' frame='true' scene='Molecular_Playground/Caspase_Dynamics/Morph2/1' align='right' caption='Conformational Dynamics between active and allosterically inhibited caspase-7 elucidate the mechanism of allostery in this important class of cysteine proteases.' />
+<applet load='Caspmorph.pdb' size='300' frame='true' scene='Molecular_Playground/Caspase_Dynamics/Morph2/2' align='right' caption='Conformational Dynamics between active and allosterically inhibited caspase-7 elucidate the mechanism of allostery in this important class of cysteine proteases.' />
 Conformational dynamics in Caspase-7 are mediated by an 'Allosteric Toggle' mechanism in which binding of allosteric inhibitor DICA to CYS 290 pushes TYR 223 into 'up' conformation forcing ARG 187 'out' into a form that is physically incompatible with substrate binding.
@@ Line 12: / Line 12: @@
 *<scene name='Molecular_Playground/Caspase_Dynamics/1f1j/2'>Caspase-7 bound to suicide inhibitor/substrate mimic DEVD-CHO</scene>, trapping protein in active/substrate bound conformation.
 *<scene name='Molecular_Playground/Caspase_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='Molecular_Playground/Caspase_Dynamics/Morph2/1'>Conformational change between substrate bound and substrate incompatible forms</scene> of Caspase-7.
+*<scene name='Molecular_Playground/Caspase_Dynamics/Morph2/2'>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.