title: Actomyosin: law and order in motility.
abstract: The crystal structures of smooth muscle and scallop striated muscle myosin have both been completed in the past 18 months. Structural studies of unconventional myosins, in particular the stunning discovery that myosin VI moves backwards on actin, are starting to have deep impact on the field and have induced new ways of thinking about actin-based motility. Sophisticated genetic, biochemical and biophysical studies were used to test and refine hypotheses of the molecular mechanism of motility that were developed in the past. Although all these studies confirmed some aspects of these hypotheses, they also raised many new unresolved questions. Much of the evidence points to the importance of the actin-myosin binding process and an associated disorder-to-order transition.
authors.affiliation: The Burnham Institute, La Jolla, 92037, USA. niels@burnham.org
authors.forename: N
authors.initials: N
authors.lastname: Volkmann
authors.forename: D
authors.initials: D
authors.lastname: Hanein
mesh_terms: D000199:Actins / Q000737:chemistry* / Q000378:metabolism*; D000205:Actomyosin / Q000737:chemistry* / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002312:Cardiomyopathy, Hypertrophic; D002384:Catalysis; D006801:Humans; D009218:Myosins / Q000737:chemistry* / Q000378:metabolism*; D009711:Nucleotides / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D000199:Actins; D009711:Nucleotides; D000255:Adenosine Triphosphate; D000205:Actomyosin; D009218:Myosins