Integrated analysis of residue coevolution and protein structure in ABC transporters.

ABSTRACT: Intraprotein side chain contacts can couple the evolutionary process of amino acid substitution at one position to that at another. This coupling, known as residue coevolution, may vary in strength. Conserved contacts thus not only define 3-dimensional protein structure, but also indicate which residue-residue interactions are crucial to a protein's function. Therefore, prediction of strongly coevolving residue-pairs helps clarify molecular mechanisms underlying function. Previously, various coevolution detectors have been employed separately to predict these pairs purely from multiple sequence alignments, while disregarding available structural information. This study introduces an integrative framework that improves the accuracy of such predictions, relative to previous approaches, by co

SUBMITTER: Gulyas-Kovacs A 

PROVIDER: S-EPMC3348156 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature