title: Structure-function analysis of the motor domain of myosin.
abstract: Motor proteins perform a wide variety of functions in all eukaryotic cells. Recent advances in the structural and mutagenic analysis of the myosin motor has led to insights into how these motors transduce chemical energy into mechanical work. This review focuses on the analysis of the effects of myosin mutations from a variety of organisms on the in vivo and in vitro properties of this ubiquitous motor and illustrates the positions of these mutations on the high-resolution three-dimensional structure of the myosin motor domain.
authors.affiliation: Department of Biochemistry, Stanford University School of Medicine, California 94305, USA.
authors.forename: K M
authors.initials: KM
authors.lastname: Ruppel
authors.forename: J A
authors.initials: JA
authors.lastname: Spudich
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008969:Molecular Sequence Data; D009218:Myosins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017421:Sequence Analysis; D013329:Structure-Activity Relationship
chemical_list: D009218:Myosins