Molecular Playground/Caspase-7 Dynamics: Difference between revisions
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New page: <applet load='Caspmorph.pdb' size='300' frame='true' align='right' caption='Toggle between active site inhibitor bound and allosterically inhibited caspase-7' /> Conformational dynamics i... |
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< | Caspases are a family of [[CBI Molecules]] being studied in the <span class="plainlinks">[http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program]</span> at UMass Amherst and on display at the <span class="plainlinks">[http://www.molecularplayground.org/ Molecular Playground]</span>. | ||
=== Caspase-7 as 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/Morph2/2' align='right' caption='Conformational Dynamics between active and allosterically inhibited caspase-7 elucidate the mechanism of allostery in this important class of cysteine proteases.' /> | |||
The cleaved termini of the large and small subunits which form the active site loop bundle become highly ordered in active | 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. | ||
The cleaved termini of the large and small subunits which form the active site loop bundle become highly ordered in active conformation, and highly disordered in allosterically inhibited form (so much so that they cannot be resolved crystallographically). | |||
=== Forms of Caspase-7 === | === Forms of Caspase-7 === | ||
*<scene name=' | *<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=' | *<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=' | *<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 for Caspase-7 === | ||
'''Molecular Playground banner:''' Conformational Dynamics between active and allosterically inhibited caspase-7 elucidate the mechanism of allostery in this important class of cysteine proteases. | '''Molecular Playground banner:''' Conformational Dynamics between active and allosterically inhibited caspase-7 elucidate the mechanism of allostery in this important class of cysteine proteases. | ||
==3D structures of caspase== | |||
[[Caspase]] | |||
==Additional Resources== | |||
For additional information, see: [[Cancer]] | |||
<br /> | |||
Latest revision as of 23:02, 3 December 2013
Caspases are a family of CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
Caspase-7 as studied in the Hardy Lab Caspase-7 as studied in the Hardy Lab
|
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.
The cleaved termini of the large and small subunits which form the active site loop bundle become highly ordered in active conformation, and highly disordered in allosterically inhibited form (so much so that they cannot be resolved crystallographically).
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.
Molecular Playground banner for Caspase-7Molecular Playground banner for Caspase-7
Molecular Playground banner: Conformational Dynamics between active and allosterically inhibited caspase-7 elucidate the mechanism of allostery in this important class of cysteine proteases.
3D structures of caspase3D structures of caspase
Additional ResourcesAdditional Resources
For additional information, see: Cancer