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User:Kristen Huber/Sandbox 1
From Proteopedia
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<applet load='1jxq' size='400' color='white' frame='true' align='right' caption='Caspase-9 Dimer' | <applet load='1jxq' size='400' color='white' frame='true' align='right' caption='Caspase-9 Dimer' | ||
| - | + | scene='User:Kristen_Huber/Sandbox_1/Caspase-9_dimer/1'>Caspase-9 Molecular Playground</scene> | |
<scene name='User:Kristen_Huber/Sandbox_1/Caspase-9_dimer/1'>Caspase-9 Molecular Playground</scene> | <scene name='User:Kristen_Huber/Sandbox_1/Caspase-9_dimer/1'>Caspase-9 Molecular Playground</scene> | ||
Revision as of 19:02, 4 May 2010
One of the 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-9 belongs to a family of "molecular scissors" called cysteine aspartate proteases. These proteases are the facilitators of apoptosis, the highly process of programmed cell death which is an important cellular process critical for normal development and stability of an organism.
Caspase-9 is regulated by controlling its multimeric state through monomer-dimer transitions. Caspase-9 exists as an inactive monomer and becomes active upon dimerization. It is in this dimeric state that caspase-9 can “cut” its intended protein partners (called substrates) at a specific amino acid sequence. X-linked inhibitors of apoptosis proteins, specifically the BIR3 domain, bind to monomeric caspase-9 to block dimerization thus preventing activation.
Structure
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