Conformational propensities of intrinsically disordered proteins influence the mechanism of binding and folding.

ABSTRACT: Intrinsically disordered proteins (IDPs) frequently function in protein interaction networks that regulate crucial cellular signaling pathways. Many IDPs undergo transitions from disordered conformational ensembles to folded structures upon binding to their cellular targets. Several possible binding mechanisms for coupled folding and binding have been identified: folding of the IDP after association with the target ("induced fit"), or binding of a prefolded state in the conformational ensemble of the IDP to the target protein ("conformational selection"), or some combination of these two extremes. The interaction of the intrinsically disordered phosphorylated kinase-inducible domain (pKID) of the cAMP-response element binding (CREB) protein with the KIX domain of a general transcriptional

SUBMITTER: Arai M 

PROVIDER: S-EPMC4534220 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature