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Troponin structure and function: a view of recent progress.

Abstract

The molecular mechanism by which Ca2+ binding and phosphorylation regulate muscle contraction through Troponin is not yet fully understood. Revealing the differences between the relaxed and active structure of cTn, as well as the conformational changes that follow phosphorylation has remained a challenge for structural biologists over the years. Here we review the current understanding of how Ca2+, phosphorylation and disease-causing mutations affect the structure and dynamics of troponin to regulate the thin filament based on electron microscopy, X-ray diffraction, NMR and molecular dynamics methodologies.

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  • Authors+Show Affiliations

    ,

    NHLI and Chemistry Departments, Imperial College London, W12 0NN, London, UK. s.marston@imperial.ac.uk.

    NHLI and Chemistry Departments, Imperial College London, W12 0NN, London, UK.

    Source

    Pub Type(s)

    Journal Article

    Language

    eng

    PubMed ID

    31030382

    Citation

    Marston, Steven, and Juan Eiros Zamora. "Troponin Structure and Function: a View of Recent Progress." Journal of Muscle Research and Cell Motility, 2019.
    Marston S, Zamora JE. Troponin structure and function: a view of recent progress. J Muscle Res Cell Motil. 2019.
    Marston, S., & Zamora, J. E. (2019). Troponin structure and function: a view of recent progress. Journal of Muscle Research and Cell Motility, doi:10.1007/s10974-019-09513-1.
    Marston S, Zamora JE. Troponin Structure and Function: a View of Recent Progress. J Muscle Res Cell Motil. 2019 Apr 27; PubMed PMID: 31030382.
    * Article titles in AMA citation format should be in sentence-case
    TY - JOUR T1 - Troponin structure and function: a view of recent progress. AU - Marston,Steven, AU - Zamora,Juan Eiros, Y1 - 2019/04/27/ PY - 2019/01/09/received PY - 2019/04/12/accepted PY - 2019/4/29/entrez PY - 2019/4/29/pubmed PY - 2019/4/29/medline KW - Ca2+ KW - Muscle regulation KW - Mutation KW - Phosphorylation KW - Thin filaments KW - Troponin JF - Journal of muscle research and cell motility JO - J. Muscle Res. Cell. Motil. N2 - The molecular mechanism by which Ca2+ binding and phosphorylation regulate muscle contraction through Troponin is not yet fully understood. Revealing the differences between the relaxed and active structure of cTn, as well as the conformational changes that follow phosphorylation has remained a challenge for structural biologists over the years. Here we review the current understanding of how Ca2+, phosphorylation and disease-causing mutations affect the structure and dynamics of troponin to regulate the thin filament based on electron microscopy, X-ray diffraction, NMR and molecular dynamics methodologies. SN - 1573-2657 UR - https://www.unboundmedicine.com/medline/citation/31030382/Troponin_structure_and_function:_a_view_of_recent_progress L2 - https://doi.org/10.1007/s10974-019-09513-1 DB - PRIME DP - Unbound Medicine ER -