Evolution of domain-peptide interactions to coadapt specificity and affinity to functional diversity.

ABSTRACT: Evolution of complexity in eukaryotic proteomes has arisen, in part, through emergence of modular independently folded domains mediating protein interactions via binding to short linear peptides in proteins. Over 30 years, structural properties and sequence preferences of these peptides have been extensively characterized. Less successful, however, were efforts to establish relationships between physicochemical properties and functions of domain-peptide interactions. To our knowledge, we have devised the first strategy to exhaustively explore the binding specificity of protein domain-peptide interactions. We applied the strategy to SH3 domains to determine the properties of their binding peptides starting from various experimental data. The strategy identified the majority (∼70%) of experi

SUBMITTER: Kelil A 

PROVIDER: S-EPMC4941456 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature