title: Kinesins and microtubules: their structures and motor mechanisms.
abstract: Atomic resolution three-dimensional structures of two oppositely directed kinesin motors - conventional kinesin and non-claret disjunctional (ncd) protein - are now available in their functional dimeric form. A detailed model of the microtubule has also been recently obtained by docking the 3.7 A structure of tubulin into a 20 A map of the microtubule. Recent structural studies of kinesin motors and their microtubule tracks are contributing to our current understanding of kinesin motor mechanisms.
authors.affiliation: Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA. sablin@msg.ucsf.edu
authors.forename: E P
authors.initials: EP
authors.lastname: Sablin
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D019281:Dimerization; D029721:Drosophila Proteins; D016547:Kinesins / Q000737:chemistry* / Q000378:metabolism*; D008870:Microtubules / Q000737:chemistry* / Q000378:metabolism*; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation
chemical_list: D029721:Drosophila Proteins; D020409:Molecular Motor Proteins; C066696:ncd protein, Drosophila; D016547:Kinesins