A novel method for protein-protein interaction site prediction using phylogenetic substitution models.

ABSTRACT: Protein-protein binding events mediate many critical biological functions in the cell. Typically, functionally important sites in proteins can be well identified by considering sequence conservation. However, protein-protein interaction sites exhibit higher sequence variation than other functional regions, such as catalytic sites of enzymes. Consequently, the mutational behavior leading to weak sequence conservation poses significant challenges to the protein-protein interaction site prediction. Here, we present a phylogenetic framework to capture critical sequence variations that favor the selection of residues essential for protein-protein binding. Through the comprehensive analysis of diverse protein families, we show that protein binding interfaces exhibit distinct amino acid substitut

SUBMITTER: La D 

PROVIDER: S-EPMC3240730 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature