Transient protein-protein interaction of the SH3-peptide complex via closely located multiple binding sites.

ABSTRACT: Protein-protein interactions play an essential role in cellular processes. Certain proteins form stable complexes with their partner proteins, whereas others function by forming transient complexes. The conventional protein-protein interaction model describes an interaction between two proteins under the assumption that a protein binds to its partner protein through a single binding site. In this study, we improved the conventional interaction model by developing a Multiple-Site (MS) model in which a protein binds to its partner protein through closely located multiple binding sites on a surface of the partner protein by transiently docking at each binding site with individual binding free energies. To test this model, we used the protein-protein interaction mediated by Src homology 3 (SH3

SUBMITTER: Hahn S 

PROVIDER: S-EPMC3310816 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature