The dock-and-coalesce mechanism for the association of a WASP disordered region with the Cdc42 GTPase.

ABSTRACT: Intrinsically disordered proteins (IDPs) play key roles in signaling and regulation. Many IDPs undergo folding upon binding to their targets. We have proposed that coupled folding and binding of IDPs generally follow a dock-and-coalesce mechanism, whereby a segment of the IDP, through diffusion, docks to its cognate subsite and, subsequently, the remaining segments coalesce around their subsites. Here, by a combination of experiment and computation, we determined the precise form of dock-and-coalesce operating in the association between the intrinsically disordered GTPase-binding domain (GBD) of the Wiskott-Aldrich Syndrome protein and the Cdc42 GTPase. The association rate constants (k_a ) were measured by stopped-flow fluorescence under various solvent conditions. k_a

SUBMITTER: Ou L 

PROVIDER: S-EPMC5643242 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature