User:Kristen Huber/Sandbox 1
From Proteopedia
(Difference between revisions)
(→Caspase-9/XIAP-BIR3 Interaction) |
|||
| Line 18: | Line 18: | ||
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. | 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. | ||
| + | |||
| + | <scene name='User:Kristen_Huber/Sandbox_1/Caspase-9_xiap_bir3_complex/2'>TextToBeDisplayed</scene> | ||
==See Also== | ==See Also== | ||
Revision as of 18:06, 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.
| |||||||||||
