Relative solvent accessible surface area predicts protein conformational changes upon binding.

ABSTRACT: Protein interactions are often accompanied by significant changes in conformation. We have analyzed the relationships between protein structures and the conformational changes they undergo upon binding. Based upon this, we introduce a simple measure, the relative solvent accessible surface area, which can be used to predict the magnitude of binding-induced conformational changes from the structures of either monomeric proteins or bound subunits. Applying this to a large set of protein complexes suggests that large conformational changes upon binding are common. In addition, we observe considerable enrichment of intrinsically disordered sequences in proteins predicted to undergo large conformational changes. Finally, we demonstrate that the relative solvent accessible surface area of monome

SUBMITTER: Marsh JA 

PROVIDER: S-EPMC3145976 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature