title: Recent progress in dynein structure and mechanism.
abstract: Dynein is a minus-end-directed microtubule motor crucial to diverse cellular processes. The unwieldy size of the molecule and the difficulty of expressing and purifying mutants have hampered mechanistic studies of dynein. Recent progress sheds light on key unsolved questions concerning how the molecule is really organized, what conformational changes accompany ATP hydrolysis and whether two or three motor domains are coordinated in their motion.
authors.affiliation: Kansai Advanced Research Center, 588-2 Iwaoka, Nishi-ku, Kobe 6512492, Japan. oiwa@po.nict.go.jp
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Oiwa
authors.forename: Hitoshi
authors.initials: H
authors.lastname: Sakakibara
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry; D000255:Adenosine Triphosphate / Q000737:chemistry; D000818:Animals; D001695:Biology / Q000639:trends; D002696:Chlamydomonas / Q000378:metabolism; D004398:Dyneins / Q000737:chemistry* / Q000502:physiology*; D005407:Flagella; D006868:Hydrolysis; D008870:Microtubules / Q000648:ultrastructure; D008954:Models, Biological; D016011:Normal Distribution; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D013768:Tetrahymena
chemical_list: D010455:Peptides; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D004398:Dyneins