title: The motor mechanism of myosin V: insights for muscle contraction.
abstract: It is 50 years since the sliding of actin and myosin filaments was proposed as the basis of force generation and shortening in striated muscle. Although this is now generally accepted, the detailed molecular mechanism of how myosin uses adenosine triphosphate to generate force during its cyclic interaction with actin is only now being unravelled. New insights have come from the unconventional myosins, especially myosin V. Myosin V is kinetically tuned to allow movement on actin filaments as a single molecule, which has led to new kinetic, mechanical and structural data that have filled in missing pieces of the actomyosin-chemo-mechanical transduction puzzle.
authors.affiliation: Department of Physiology, University of Pennsylvania School of Medicine, A700 Richards Building, 3700 Hamilton Walk, Philadelphia, PA 19104-6085, USA. isweeney@mail.med.upenn.edu
authors.forename: H Lee
authors.initials: HL
authors.lastname: Sweeney
authors.forename: Anne
authors.initials: A
authors.lastname: Houdusse
mesh_terms: D000199:Actins / Q000378:metabolism / Q000502:physiology*; D000818:Animals; D001665:Binding Sites; D001696:Biomechanical Phenomena; D007700:Kinetics; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000502:physiology*; D009119:Muscle Contraction / Q000502:physiology*; D018482:Muscle, Skeletal / Q000502:physiology*; D024701:Myosin Type V / Q000378:metabolism / Q000502:physiology*; D011487:Protein Conformation
chemical_list: D000199:Actins; D020409:Molecular Motor Proteins; D024701:Myosin Type V