title: Structure of the actin-myosin complex and its implications for muscle contraction.
abstract: Muscle contraction consists of a cyclical interaction between myosin and actin driven by the concomitant hydrolysis of adenosine triphosphate (ATP). A model for the rigor complex of F actin and the myosin head was obtained by combining the molecular structures of the individual proteins with the low-resolution electron density maps of the complex derived by cryo-electron microscopy and image analysis. The spatial relation between the ATP binding pocket on myosin and the major contact area on actin suggests a working hypothesis for the crossbridge cycle that is consistent with previous independent structural and biochemical studies.
authors.affiliation: Department of Biochemistry, University of Wisconsin, Madison 53705.
authors.forename: I
authors.initials: I
authors.lastname: Rayment
authors.forename: H M
authors.initials: HM
authors.lastname: Holden
authors.forename: M
authors.initials: M
authors.lastname: Whittaker
authors.forename: C B
authors.initials: CB
authors.lastname: Yohn
authors.forename: M
authors.initials: M
authors.lastname: Lorenz
authors.forename: K C
authors.initials: KC
authors.lastname: Holmes
authors.forename: R A
authors.initials: RA
authors.lastname: Milligan
mesh_terms: D000199:Actins / Q000737:chemistry* / Q000378:metabolism; D000205:Actomyosin / Q000737:chemistry* / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D007091:Image Processing, Computer-Assisted; D008958:Models, Molecular; D009119:Muscle Contraction; D015879:Myosin Subfragments / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D014961:X-Ray Diffraction
chemical_list: D000199:Actins; D015879:Myosin Subfragments; D000255:Adenosine Triphosphate; D000205:Actomyosin