Probing the local dynamics of nucleotide-binding pocket coupled to the global dynamics: myosin versus kinesin.

ABSTRACT: Based on the elastic network model, we develop a new analysis for protein complexes, which probes the local dynamics of a subsystem that is elastically coupled to a fluctuating environment. This method is applied to a comparative dynamical analysis of the nucleotide-binding pocket of two motor proteins-myosins and kinesins. In myosins, the observed structural changes in the nucleotide-pocket from the transition state to the rigorlike state are dominated by the lowest normal mode that involves significant movements in both switch I and switch II; in kinesins, the measured conformational changes in the nucleotide-pocket are also dominated by the lowest mode, which, however, only involves large movement in switch I. We then compute the global structural changes induced by the nucleotide-pocke

SUBMITTER: Zheng W 

PROVIDER: S-EPMC1366515 | biostudies-literature | 2005 Jul

REPOSITORIES: biostudies-literature