Crystallography of cargo-mediated activation mechanism of molecular motor proteins, kinesin superfamily members KIF5 and KIF13B

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Kinesins are molecular motors that share a common structural core with myosins and G proteins and play diverse roles in organelle transport, cell division, and cell movement. Kinesin motors use the chemical energy derived from the hydrolysis of adenosine tri-phosphate to generate force for a unidirectional movement along the microtubule highway and transport cargoes (vesicles, protein complexes, RNAs and mitochondria). Regulation of kinesin motors is important because a constantly active motor would consume futile adenosine tri-phosphate and move to the tips of microtubules without loaded cargoes. Both Kinesin-1 and KIF13B cycle between two conformations: the folded, inhibited state and the extended, activated state. The proposed studies will give a first look at the structures of the cargo binding domains and provide a basis for explaining how kinesin is regulated by the cargo binding domains.