Co-Evolution of Intrinsically Disordered Proteins with Folded Partners Witnessed by Evolutionary Couplings.

ABSTRACT: Although improved strategies for the detection and analysis of evolutionary couplings (ECs) between protein residues already enable the prediction of protein structures and interactions, they are mostly restricted to conserved and well-folded proteins. Whereas intrinsically disordered proteins (IDPs) are central to cellular interaction networks, due to the lack of strict structural constraints, they undergo faster evolutionary changes than folded domains. This makes the reliable identification and alignment of IDP homologs difficult, which led to IDPs being omitted in most large-scale residue co-variation analyses. By preforming a dedicated analysis of phylogenetically widespread bacterial IDP⁻partner interactions, here we demonstrate that partner binding imposes constraints on IDP sequenc

SUBMITTER: Pancsa R 

PROVIDER: S-EPMC6274761 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature