title: The myosin mesa and a possible unifying hypothesis for the molecular basis of human hypertrophic cardiomyopathy.
abstract: No matter how many times one explores the structure of the myosin molecule, there is always something new to discover. Here, I describe the myosin mesa, a structural feature of the motor domain that has the characteristics of a binding domain for another protein, possibly myosin-binding protein C (MyBP-C). Interestingly, many well-known hypertrophic cardiomyopathy (HCM) mutations lie along this surface and may affect the putative interactions proposed here. A potential unifying hypothesis for the molecular basis of human hypertrophic cardiomyopathy is discussed here. It involves increased power output of the cardiac muscle as a result of HCM mutations causing the release of inhibition by myosin binding protein C.
authors.affiliation: *Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305, U.S.A.
authors.forename: James A
authors.initials: JA
authors.lastname: Spudich
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002312:Cardiomyopathy, Hypertrophic / Q000378:metabolism*; D002352:Carrier Proteins / Q000737:chemistry / Q000502:physiology; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009218:Myosins / Q000737:chemistry* / Q000502:physiology; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D000099163:Myosin Binding Protein C
chemical_list: D002352:Carrier Proteins; D009218:Myosins; D000099163:Myosin Binding Protein C