User:Kristen Huber/Sandbox 1

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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

• http://www.pdb.org/pdb/explore/explore.do?structureId=1JXQ Cleaved Caspase-9 Dimer ( PDB ID ; 1JXQ) at RCSB PDB]
• http://www.pdb.org/pdb/explore/explore.do?structureId=1NW9 Caspase-9/XIAP BIR3 Inhibitory Complex ( PDB ID ; 1NW9) at RCSB PDB]

References

• [1] Renatus, M.; Stennicke, H. R.; Scott, F. L.; Liddington, R. C.; Salvesen, G. S., Dimer formation drives the activation of the cell death protease caspase 9. PNAS 2001, 98, (25), 14250.
• [2] Shiozaki, E. N.; Chai, J.; Rigotti, D. J.; Riedl, S. J.; Li, P.; Srinivasula, S. M.; Alnemri, E. S.; Fairman, R.; Shi, Y., Mechanism of XIAP-mediated inhibition of caspase-9. Molecular Cell 2003, 11, (2), 519-527.