Nucleotide-free structures of KIF20A illuminate atypical mechanochemistry in this kinesin-6.

ABSTRACT: KIF20A is a critical kinesin for cell division and a promising anti-cancer drug target. The mechanisms underlying its cellular roles remain elusive. Interestingly, unusual coupling between the nucleotide- and microtubule-binding sites of this kinesin-6 has been reported, but little is known about how its divergent sequence leads to atypical motility properties. We present here the first high-resolution structure of its motor domain that delineates the highly unusual structural features of this motor, including a long L6 insertion that integrates into the core of the motor domain and that drastically affects allostery and ATPase activity. Together with the high-resolution cryo-electron microscopy microtubule-bound KIF20A structure that reveals the microtubule-binding interface, we dissect t

SUBMITTER: Ranaivoson FM 

PROVIDER: S-EPMC10508983 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature