The kinesin motor proteins generate directional movement along microtubules
and are involved in many vital processes, including cell division, in euka
ryotes, The kinesin superfamily is characterized by a conserved motor domai
n of similar to 320 residues. Dimeric constructs of N and C class kinesins,
with the motor domains at opposite ends of the heavy chain, move towards m
icrotubule plus and minus ends, respectively. Their crystal structures diff
er mainly in the region linking the motor domain core to the a-helical coil
ed coil dimerization domain. Chimeric kinesins show that regions outside of
the motor domain core determine the direction of movement and mutations in
the linker region have a strong effect on motility, Recent work on chimera
s and mutants is discussed in a structural context giving insights to possi
ble molecular mechanisms of kinesin directionality and motility.