Abstract

Spatial and temporal regulation of kinesin activity is essential for a diversity of eukaryotic cellular processes including mitosis and intracellular cargo distribution. Kinesin binding protein (KBP), derived from the causal gene in Goldberg-Shprintzen syndrome, binds a select subset of kinesin motor domains and inhibits their microtubule attachment, however the structural mechanisms behind this activity have been unclear. Here we use cryo-electron microscopy to reveal the structure of KBP and of a KBP-kinesin motor domain complex.

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