Anchor Effect of Interactions Between Kinesin's Nucleotide-Binding Pocket and Microtubule.

ABSTRACT: Microtubule not only provides the track for kinesin but also modulates kinesin's mechanochemical cycle. Microtubule binding greatly increases the rates of two chemical steps occurring inside the nucleotide-binding pocket (NBP) of kinesin, i.e., ATP hydrolysis and ADP release. Kinesin neck linker docking (the key force-generation step) is initiated by the motor head rotation induced by ATP binding which needs an anchor provided by microtubule. These functions of microtubule can only be accomplished through interactions with kinesin. Based on the newly obtained crystal structures of kinesin-microtubule complexes, we investigate the interactions between kinesin's NBP and microtubule using molecular dynamics simulations. We find that the N-3 motif of NBP has direct interactions with a group of

SUBMITTER: Jin Y 

PROVIDER: S-EPMC6816667 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature