User:Kristen Huber/Sandbox 1
From Proteopedia
(Difference between revisions)
(New page: One of the CBI Molecules being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at th...) |
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One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | ||
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| - | <applet load='1jxq' size='400' color='white' frame='true' align='right' caption='Dimeric Caspase-9 (Active)' | ||
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| - | Molecular Playground banner: Cleaved Caspase-9, the active dimer. | ||
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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. | 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. | ||
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==Structure== | ==Structure== | ||
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==Caspase-9/XIAP-BIR3 Interaction== | ==Caspase-9/XIAP-BIR3 Interaction== | ||
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| + | The protein-protein interface of the Caspase-9/XIAP BIR3 complex is dominated by a high level of shape complimentarily, a large collection of van der Walls contacts, and 11 intermolecular hydrogen bonds scattered throughout the entire 2200 Å2 interface of the complex [2]. This interaction prevents caspase-9 from dimerizing as well as prevents the organization of the loop bundle thus making the molecule inactive. | ||
==See Also== | ==See Also== | ||
Revision as of 18:00, 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.
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