Homology inference of protein-protein interactions via conserved binding sites.

ABSTRACT: The coverage and reliability of protein-protein interactions determined by high-throughput experiments still needs to be improved, especially for higher organisms, therefore the question persists, how interactions can be verified and predicted by computational approaches using available data on protein structural complexes. Recently we developed an approach called IBIS (Inferred Biomolecular Interaction Server) to predict and annotate protein-protein binding sites and interaction partners, which is based on the assumption that the structural location and sequence patterns of protein-protein binding sites are conserved between close homologs. In this study first we confirmed high accuracy of our method and found that its accuracy depends critically on the usage of all available data on stru

SUBMITTER: Tyagi M 

PROVIDER: S-EPMC3269416 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature