Conservation and relative importance of residues across protein-protein interfaces.

ABSTRACT: A core region surrounded by a rim characterizes biological interfaces. We ascertain the importance of the core by showing the sequence entropies of the residues comprising the core to be smaller than those in the rim. Such a distinction is not seen in the 2-fold-related, nonphysiological interfaces formed in crystal lattices of monomeric proteins, thereby providing a procedure for characterizing the oligomeric state from crystal structures of protein molecules. This method is better than those that rely on the comparison of the sequence entropies in the interface and the rest of the protein surface, especially in cases where the surface harbors additional binding sites. To a good approximation there is a correlation between the accessible surface area lost because of complexation and Delta

SUBMITTER: Guharoy M 

PROVIDER: S-EPMC1266102 | biostudies-literature | 2005 Oct

REPOSITORIES: biostudies-literature