title: Structure and dynamics of molecular motors.
abstract: The structures of the oppositely directed microtubule motors kinesin and ncd have been solved to atomic resolution. The two structures are very similar and are also homologous to myosin. Myosins and kinesins differ kinetically but, tantalizingly, cryoelectron microscopy has recently revealed that both structures may tilt during ADP release. Such evidence suggests that the two motor families use common structural mechanisms.
authors.affiliation: MRC Laboratory of Molecular Biology, MRC Centre, Hills Road, Cambridge, CB2 2QH, UK. laa@mrc-lmb.cam.ac.uk
authors.forename: L A
authors.initials: LA
authors.lastname: Amos
authors.forename: R A
authors.initials: RA
authors.lastname: Cross
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins; D004398:Dyneins / Q000737:chemistry; D016547:Kinesins / Q000737:chemistry; D008868:Microtubule Proteins / Q000737:chemistry*; D008958:Models, Molecular; D009218:Myosins / Q000737:chemistry*; D011487:Protein Conformation
chemical_list: D029721:Drosophila Proteins; D008868:Microtubule Proteins; C066696:ncd protein, Drosophila; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D009218:Myosins; D004398:Dyneins; D016547:Kinesins