title: The dynein heavy chain: structure, mechanics and evolution.
abstract: The translocation of dynein along microtubules is the basis for a variety of essential cellular movements. Despite a general domain organization that is found in all the cytoskeletal motors, there are structural features of dynein that set it apart from the other motors. These include a track-binding site that is located at the tip of a long projection, and six nucleotide-binding modules that together form the globular head of dynein. These unique features suggest that dynein produces movement by a mechanism that is different from that used by the other motors.
authors.affiliation: Dept of Biological Sciences, Purdue University, Lilly Hall, West Lafayette, IN 47907-1392, USA. dasai@bilbo.bio.purdue.edu
authors.forename: D J
authors.initials: DJ
authors.lastname: Asai
authors.forename: M P
authors.initials: MP
authors.lastname: Koonce
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004398:Dyneins / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D019143:Evolution, Molecular; D006801:Humans; D008870:Microtubules / Q000378:metabolism; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000502:physiology*; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D020409:Molecular Motor Proteins; D004398:Dyneins