title: Dynein structure and function.
abstract: The structure of dynein isolated from several sources follows the pattern first observed with Tetrahymena 22S dynein, which has three globular heads attached by three flexible strands to a root-like base. Recent biochemical data indicate that there is one ATPase site on each dynein head and that all three heads interact with microtubules in an ATP-sensitive manner. Accordingly, images of dynein in situ can be interpreted in terms of a model for crossbridge action where the roots of the bouquet anchor the dynein to the A-tubule and all three heads reach out to interact with the B-tubule in an ATP-dependent reaction to produce a force for sliding.
mesh_terms: D000251:Adenosine Triphosphatases / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000502:physiology; D000818:Animals; D001665:Binding Sites; D004398:Dyneins / Q000502:physiology*; D008870:Microtubules / Q000502:physiology* / Q000648:ultrastructure; D008954:Models, Biological; D013329:Structure-Activity Relationship
chemical_list: D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D004398:Dyneins