• Title of article

    Crystal Structure of the C1 domain of Cardiac Myosin Binding Protein-C: Implications for Hypertrophic Cardiomyopathy

  • Author/Authors

    Lata Govada، نويسنده , , Liz Carpenter، نويسنده , , Paula C.A. da Fonseca، نويسنده , , John R. Helliwell، نويسنده , , Pierre Rizkallah، نويسنده , , Emily Flashman، نويسنده , , Naomi E. Chayen، نويسنده , , Charles Redwood، نويسنده , , John M. Squire، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2008
  • Pages
    11
  • From page
    387
  • To page
    397
  • Abstract
    C-protein is a major component of skeletal and cardiac muscle thick filaments. Mutations in the gene encoding cardiac C-protein [cardiac myosin binding protein-C (cMyBP-C)] are one of the principal causes of hypertrophic cardiomyopathy. cMyBP-C is a string of globular domains including eight immunoglobulin-like and three fibronectin-like domains termed C0–C10. It binds to myosin and titin, and probably to actin, and may have both a structural and a regulatory role in muscle function. To help to understand the pathology of the known mutations, we have solved the structure of the immunoglobulin-like C1 domain of MyBP-C by X-ray crystallography to a resolution of 1.55 Å. Mutations associated with hypertrophic cardiomyopathy are clustered at one end towards the C-terminus, close to the important C1C2 linker, where they alter the structural integrity of this region and its interactions.
  • Keywords
    C-protein , hypertrophic cardiomyopathy , IgI domain structure , muscle regulation , MyBP-C C1 domain
  • Journal title
    Journal of Molecular Biology
  • Serial Year
    2008
  • Journal title
    Journal of Molecular Biology
  • Record number

    1256522