The stalk domain of kinesin-1 is responsible for:
Domain architecture of kinesin-1 reveals clear division of labor essential for processive dimer motor function. N terminal globular motor domain about 340 amino acids contains P loop ATPase site switch I II microtubule binding interface and neck linker for mechanochemistry converting ATP hydrolysis to mechanical step. Immediately C terminal lies neck coiled coil ensuring dimerization of motor domains upon folding critical for hand over hand coordination followed by elongated stalk extending about 50 nm formed by interrupted coiled coil heptad repeats left handed supercoils stabilizing heavy ch
Ref: Hirokawa & Noda, Physiol Rev 2008 – Kinesin-1 stalk coiled coil mediated dimerization domain function.
