Structural links to kinesin directionality and movement

Citation
Rh. Wade et F. Kozielski, Structural links to kinesin directionality and movement, NAT ST BIOL, 7(6), 2000, pp. 456-460
Citations number
35
Categorie Soggetti
Biochemistry & Biophysics
Journal title
NATURE STRUCTURAL BIOLOGY
ISSN journal
10728368 → ACNP
Volume
7
Issue
6
Year of publication
2000
Pages
456 - 460
Database
ISI
SICI code
1072-8368(200006)7:6<456:SLTKDA>2.0.ZU;2-H
Abstract
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.