Investigation into Early Steps of Actin Recognition by the Intrinsically Disordered N-WASP Domain V.

ABSTRACT: Cellular regulation or signaling processes are mediated by many proteins which often have one or several intrinsically disordered regions (IDRs). These IDRs generally serve as binders to different proteins with high specificity. In many cases, IDRs undergo a disorder-to-order transition upon binding, following a mechanism between two possible pathways, the induced fit or the conformational selection. Since these mechanisms contribute differently to the kinetics of IDR associations, it is important to investigate them in order to gain insight into the physical factors that determine the biomolecular recognition process. The verprolin homology domain (V) of the Neural Wiskott-Aldrich Syndrome Protein (N-WASP), involved in the regulation of actin polymerization, is a typical example of IDR. I

SUBMITTER: Chan-Yao-Chong M 

PROVIDER: S-EPMC6770570 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature