title: Determinants of motor polarity in the kinesin proteins.
abstract: Many of the proteins that are members of the kinesin family of microtubule motor proteins are plus-end motors; however, a few of the kinesin proteins have now been found to be minus-end microtubule motors. Overall structural features of the proteins can be used to identify further kinesins that are likely to be minus-end motors. Structural or biochemical differences that may serve as the basis of the "reversed" polarity of a unique subset of the kinesin proteins are discussed.
authors.affiliation: Department of Microbiology, Duke University Medical Center, Durham, North Carolina 27710, USA.
authors.forename: S A
authors.initials: SA
authors.lastname: Endow
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D055592:Biophysical Phenomena; D001703:Biophysics; D006868:Hydrolysis; D066298:In Vitro Techniques; D016547:Kinesins / Q000737:chemistry / Q000502:physiology*; D008870:Microtubules / Q000502:physiology; D008954:Models, Biological; D015394:Molecular Structure; D009068:Movement / Q000502:physiology; D014404:Tubulin / Q000737:chemistry
chemical_list: D014404:Tubulin; D000255:Adenosine Triphosphate; D016547:Kinesins