Structural similarity enhances interaction propensity of proteins.

ABSTRACT: We study statistical properties of interacting protein-like surfaces and predict two strong, related effects: (i) statistically enhanced self-attraction of proteins; (ii) statistically enhanced attraction of proteins with similar structures. The effects originate in the fact that the probability to find a pattern self-match between two identical, even randomly organized interacting protein surfaces is always higher compared with the probability for a pattern match between two different, promiscuous protein surfaces. This theoretical finding explains statistical prevalence of homodimers in protein-protein interaction networks reported earlier. Further, our findings are confirmed by the analysis of curated database of protein complexes that showed highly statistically significant overreprese

SUBMITTER: Lukatsky DB 

PROVIDER: S-EPMC2735088 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature