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Structural basis of allosteric interactions among Ca2+-binding sites in a K+ channel RCK domain

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  • Frank J. Smith

    (Temple University School of Medicine)

  • Victor P.T. Pau

    (Temple University School of Medicine
    Present address: Department of Physiology, University of Pennsylvania Perelman School of Medicine, 3700 Hamilton Walk, Philadelphia, Pennsylvania 19104, USA)

  • Gino Cingolani

    (Thomas Jefferson University)

  • Brad S. Rothberg

    (Temple University School of Medicine)

Abstract

Ligand binding sites within proteins can interact by allosteric mechanisms to modulate binding affinities and control protein function. Here we present crystal structures of the regulator of K+ conductance (RCK) domain from a K+ channel, MthK, which reveal the structural basis of allosteric coupling between two Ca2+ regulatory sites within the domain. Comparison of RCK domain crystal structures in a range of conformations and with different numbers of regulatory Ca2+ ions bound, combined with complementary electrophysiological analysis of channel gating, suggests chemical interactions that are important for modulation of ligand binding and subsequent channel opening.

Suggested Citation

  • Frank J. Smith & Victor P.T. Pau & Gino Cingolani & Brad S. Rothberg, 2013. "Structural basis of allosteric interactions among Ca2+-binding sites in a K+ channel RCK domain," Nature Communications, Nature, vol. 4(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3621
    DOI: 10.1038/ncomms3621
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    1. Wesley Tien Chiang & Yao-Kai Chang & Wei-Han Hui & Shu-Wei Chang & Chen-Yi Liao & Yi-Chuan Chang & Chun-Jung Chen & Wei-Chen Wang & Chien-Chen Lai & Chun-Hsiung Wang & Siou-Ying Luo & Ya-Ping Huang & , 2024. "Structural basis and synergism of ATP and Na+ activation in bacterial K+ uptake system KtrAB," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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