2vof
From Proteopedia
STRUCTURE OF MOUSE A1 BOUND TO THE PUMA BH3-DOMAIN
Overview
Apoptotic pathways are regulated by protein-protein interactions. Interaction of the BH3 domains of proapoptotic Bcl-2 family proteins with the hydrophobic groove of prosurvival proteins is critical. Whereas some BH3 domains bind in a promiscuous manner, others exhibit considerable selectivity and the sequence characteristics that distinguish these activities are unclear. In this study, crystal structures of complexes between the prosurvival protein A1 and the BH3 domains from Puma, Bmf, Bak, and Bid have been solved. The structure of A1 is similar to that of other prosurvival proteins, although features, such as an acidic patch in the binding groove, may allow specific therapeutic modulation of apoptosis. Significant conformational plasticity was observed in the intermolecular interactions and these differences explain some of the variation in affinity. This study, in combination with published data, suggests that interactions between conserved residues demarcate optimal binding.
About this Structure
2VOF is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structural plasticity underpins promiscuous binding of the prosurvival protein A1., Smits C, Czabotar PE, Hinds MG, Day CL, Structure. 2008 May;16(5):818-29. PMID:18462686 Page seeded by OCA on Thu May 22 22:32:18 2008
