A computational method for the analysis and prediction of protein:phosphopeptide-binding sites.

ABSTRACT: Phosphopeptide-binding domains, including the FHA, SH2, WW, WD40, MH2, and Polo-box domains, as well as the 14-3-3 proteins, exert control functions in important processes such as cell growth, division, differentiation, and apoptosis. Structures and mechanisms of phosphopeptide binding are generally diverse, revealing few general principles. A computational method for analysis of phosphopeptide-binding domains was therefore developed to elucidate the physical and chemical nature of phosphopeptide binding, given this lack of structural similarity. The surfaces of nine phosphopeptide-binding proteins, representing seven distinct classes of phosphopeptide-binding modules, were discretized, and encoded with information about amino acid identity, surface curvature, and electrostatic potential a

SUBMITTER: Joughin BA 

PROVIDER: S-EPMC2253325 | biostudies-literature | 2005 Jan

REPOSITORIES: biostudies-literature