Structural diversity of calmodulin binding to its target sites

Authors

  • Henning Tidow,

    Corresponding author
    1. Centre for Membrane Pumps in Cells and Disease – PUMPkin, Aarhus University, Denmark
    2. Department of Molecular Biology and Genetics, Aarhus University, Denmark
    • Correspondence

      H. Tidow, Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10c, DK-8000 Aarhus C, Denmark

      Tel: +45 2899 2295

      E-mail: het@mb.au.dk

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  • Poul Nissen

    1. Centre for Membrane Pumps in Cells and Disease – PUMPkin, Aarhus University, Denmark
    2. Department of Molecular Biology and Genetics, Aarhus University, Denmark
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Abstract

Calmodulin (CaM) is a ubiquitous, highly conserved, eukaryotic protein that binds to and regulates a number of diverse target proteins involved in different functions such as metabolism, muscle contraction, apoptosis, memory, inflammation and the immune response. In this minireview, we analyze the large number of CaM-complex structures deposited in the Protein Data Bank (i.e. crystal and nuclear magnetic resonance structures) to gain insight into the structural diversity of CaM-binding sites and mechanisms, such as those for CaM-activated protein kinases and phosphatases, voltage-gated Ca2+-channels and the plasma membrane Ca2+-ATPase.

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