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Crystal structure and molecular interactions of tropomyosin

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Abstract

The three-dimensional structure of tropomyosin filaments has been determined by X-ray crystallography. The ends of the molecules were located by reference to the single pair of cysteine residues. Departures from the α-helical-coiled coil conformation may occur in localised domains along the molecule as well as at the overlapping ends.

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Author notes

  1. E. E. Lattman

    Present address: Department of Biophysics, Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205

  2. P. Cummins

    Present address: Department of Cardiovascular Medicine, University of Birmingham, Queen Elizabeth Hospital, Birmingham, UK

Authors and Affiliations

  1. Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, 02154

    G. N. Phillips Jr, E. E. Lattman, P. Cummins, K. Y. Lee & C. Cohen

Authors
  1. G. N. Phillips Jr
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  2. E. E. Lattman
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  3. P. Cummins
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  4. K. Y. Lee
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  5. C. Cohen
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Phillips, G., Lattman, E., Cummins, P. et al. Crystal structure and molecular interactions of tropomyosin. Nature 278, 413–417 (1979). https://doi.org/10.1038/278413a0

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  • DOI: https://doi.org/10.1038/278413a0

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