Crystal structure and molecular interactions of tropomyosin

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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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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