On the importance of polar interactions for complexes containing intrinsically disordered proteins.

ABSTRACT: There is a growing recognition for the importance of proteins with large intrinsically disordered (ID) segments in cell signaling and regulation. ID segments in these proteins often harbor regions that mediate molecular recognition. Coupled folding and binding of the recognition regions has been proposed to confer high specificity to interactions involving ID segments. However, researchers recently questioned the origin of the interaction specificity of ID proteins because of the overrepresentation of hydrophobic residues in their interaction interfaces. Here, we focused on the role of polar and charged residues in interactions mediated by ID segments. Making use of the extended nature of most ID segments when in complex with globular proteins, we first identified large numbers of complexe

SUBMITTER: Wong ET 

PROVIDER: S-EPMC3749945 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature