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Calcium-induced conformational transition revealed by the solution structure of apo calmodulin

Nature Structural Biology volume 2, pages 758–767 (1995)Cite this article

Abstract

The solution structure of Ca2+-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca2+-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36°–44°. This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition. Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G are likely responsible for the cooperative Ca2+-binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains.

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  1. Mingjie Zhang

    Present address: Department of Biochemistry, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong

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  1. Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 500 Sherbourne Street, Toronto, Ontario, M4X 1K9, Canada

    Toshiyuki Tanaka & Mitsuhiko Ikura

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Zhang, M., Tanaka, T. & Ikura, M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat Struct Mol Biol 2, 758–767 (1995). https://doi.org/10.1038/nsb0995-758

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