Functional Advantages of Conserved Intrinsic Disorder in RNA-Binding Proteins.

ABSTRACT: Proteins form large macromolecular assemblies with RNA that govern essential molecular processes. RNA-binding proteins have often been associated with conformational flexibility, yet the extent and functional implications of their intrinsic disorder have never been fully assessed. Here, through large-scale analysis of comprehensive protein sequence and structure datasets we demonstrate the prevalence of intrinsic structural disorder in RNA-binding proteins and domains. We addressed their functionality through a quantitative description of the evolutionary conservation of disordered segments involved in binding, and investigated the structural implications of flexibility in terms of conformational stability and interface formation. We conclude that the functional role of intrinsically disor

SUBMITTER: Varadi M 

PROVIDER: S-EPMC4595337 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature