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Structure of the regulatory domain of scallop myosin at 2.8 Ä resolution

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Abstract

The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 Å resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca2+-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.

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Author notes

  1. C. Cohen: To whom correspondence should be addressed

Authors and Affiliations

  1. Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts, 02254-9110, USA

    X. Xie, D. H. Harrison & C. Cohen

  2. Max Planck Institut für Medizinische Forschung, D-6900, Heidelberg, Germany

    I. Schlichting

  3. Biology Department, Brookhaven National Laboratory, Upton, New York, 11973, USA

    R. M. Sweet

  4. Department of Biology, Brandeis University, Waltham, Massachusetts, 02254-9110, USA

    V. N. Kalabokis & A. G. Szent-Györgyi

Authors
  1. X. Xie
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  2. D. H. Harrison
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  3. I. Schlichting
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  4. R. M. Sweet
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  5. V. N. Kalabokis
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  6. A. G. Szent-Györgyi
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  7. C. Cohen
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Xie, X., Harrison, D., Schlichting, I. et al. Structure of the regulatory domain of scallop myosin at 2.8 Ä resolution. Nature 368, 306–312 (1994). https://doi.org/10.1038/368306a0

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  • DOI: https://doi.org/10.1038/368306a0

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