Molecular Playground/Caspase-7 Dynamics: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
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>. | 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>. | ||
<!-- expand here--> | |||
=== Caspase-7 as studied in <span class="plainlinks">[http://www.chem.umass.edu/~jhardy/ the Hardy Lab] </span>=== | === Caspase-7 as studied in <span class="plainlinks">[http://www.chem.umass.edu/~jhardy/ the Hardy Lab] </span>=== | ||
| Line 19: | Line 19: | ||
'''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. | ||
<!-- or expand here--> | |||
<!-- or where ever--> | |||
Revision as of 21:11, 4 May 2010
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.