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X-ray analysis reveals conformational adaptation of the linker in functional calmodulin mutants

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Crystal structures of target peptide bound Ca2+-calmodulin linker helix mutants with the helix shortened by two or three residues, or replaced by the longer troponin C central helix, show that the major calmodulin-target structure is preserved at the expense of linker conformation.

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Authors and Affiliations

  1. Howard Hughes Medical Institute, Baylor College of Medicine, One Baylor Plaza, Houston, Texas, 77030, USA

    William E. Meador & Florante A. Quiocho

  2. Department of Medicine, Duke University Medical School, Durham, North Carolina, 27719, USA

    Samuel E. George

  3. Department of Pharmacology, Duke University Medical School, Durham, North Carolina, 27719, USA

    Anthony R. Means

  4. Department of Biochemistry, Baylor College of Medicine, One Baylor Plaza, Houston, Texas, 77030, USA

    Florante A. Quiocho

Authors
  1. William E. Meador
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  2. Samuel E. George
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  3. Anthony R. Means
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  4. Florante A. Quiocho
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Meador, W., George, S., Means, A. et al. X-ray analysis reveals conformational adaptation of the linker in functional calmodulin mutants. Nat Struct Mol Biol 2, 943–945 (1995). https://doi.org/10.1038/nsb1195-943

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