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Three-dimensional structure of calmodulin

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Abstract

The three-dimensional structure of calmodulin has been determined crystallographically at 3.0 Å resolution. The molecule consists of two globular lobes connected by a long exposed α-helix. Each lobe binds two calcium ions through helix–loop–helix domains similar to those of other calcium-binding proteins. The long helix between the lobes may be involved in interactions of calmodulin with drugs and various proteins.

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Author notes

  1. John S. Sack

    Present address: Department of Biochemistry, Rice University, Houston, Texas, 77251, USA

Authors and Affiliations

  1. Department of Pathology, University of Alabama at Birmingham, University Station, Birmingham, Alabama, 35294, USA

    William J. Cook

  2. Department of Biochemistry, University of Alabama at Birmingham, University Station, Birmingham, Alabama, 35294, USA

    Charles E. Bugg

  3. Comprehensive Cancer Center, University of Alabama at Birmingham, University Station, Birmingham, Alabama, 35294, USA

    Y. Sudhakar Babu, John S. Sack, Trevor J. Greenhough, Charles E. Bugg & William J. Cook

  4. Institute of Dental Research, University of Alabama at Birmingham, University Station, Birmingham, Alabama, 35294, USA

    Y. Sudhakar Babu, Trevor J. Greenhough, Charles E. Bugg & William J. Cook

  5. Department of Cell Biology, Baylor College of Medicine, Houston, Texas, 77030, USA

    Anthony R. Means

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  1. Y. Sudhakar Babu
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  2. John S. Sack
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  3. Trevor J. Greenhough
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  5. Anthony R. Means
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  6. William J. Cook
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Babu, Y., Sack, J., Greenhough, T. et al. Three-dimensional structure of calmodulin. Nature 315, 37–40 (1985). https://doi.org/10.1038/315037a0

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  • DOI: https://doi.org/10.1038/315037a0

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