Conservation of coevolving protein interfaces bridges prokaryote-eukaryote homologies in the twilight zone.

ABSTRACT: Protein-protein interactions are fundamental for the proper functioning of the cell. As a result, protein interaction surfaces are subject to strong evolutionary constraints. Recent developments have shown that residue coevolution provides accurate predictions of heterodimeric protein interfaces from sequence information. So far these approaches have been limited to the analysis of families of prokaryotic complexes for which large multiple sequence alignments of homologous sequences can be compiled. We explore the hypothesis that coevolution points to structurally conserved contacts at protein-protein interfaces, which can be reliably projected to homologous complexes with distantly related sequences. We introduce a domain-centered protocol to study the interplay between residue coevolutio

SUBMITTER: Rodriguez-Rivas J 

PROVIDER: S-EPMC5206536 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature