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Structural basis for the coupling between activation and inactivation gates in K+ channels

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  • Luis G. Cuello

    (The University of Chicago
    Present address: Department of Cell Physiology and Molecular Biophysics, Texas Tech University, Lubbock, Texas 79430, USA (L.G.C, D.M.C.); D. E. Shaw Research, Hyderabad 500034, India (V.J.); D. E. Shaw Research, New York, New York 10036, USA (A.C.P.).)

  • Vishwanath Jogini

    (The University of Chicago
    Present address: Department of Cell Physiology and Molecular Biophysics, Texas Tech University, Lubbock, Texas 79430, USA (L.G.C, D.M.C.); D. E. Shaw Research, Hyderabad 500034, India (V.J.); D. E. Shaw Research, New York, New York 10036, USA (A.C.P.).)

  • D. Marien Cortes

    (The University of Chicago
    Present address: Department of Cell Physiology and Molecular Biophysics, Texas Tech University, Lubbock, Texas 79430, USA (L.G.C, D.M.C.); D. E. Shaw Research, Hyderabad 500034, India (V.J.); D. E. Shaw Research, New York, New York 10036, USA (A.C.P.).)

  • Albert C. Pan

    (The University of Chicago
    Present address: Department of Cell Physiology and Molecular Biophysics, Texas Tech University, Lubbock, Texas 79430, USA (L.G.C, D.M.C.); D. E. Shaw Research, Hyderabad 500034, India (V.J.); D. E. Shaw Research, New York, New York 10036, USA (A.C.P.).)

  • Dominique G. Gagnon

    (The University of Chicago)

  • Olivier Dalmas

    (The University of Chicago)

  • Julio F. Cordero-Morales

    (The University of Chicago)

  • Sudha Chakrapani

    (The University of Chicago)

  • Benoît Roux

    (The University of Chicago
    Institute for Biophysical Dynamics, The University of Chicago)

  • Eduardo Perozo

    (The University of Chicago
    Institute for Biophysical Dynamics, The University of Chicago)

Abstract

Potassium channels: the active-to-inactive switch Switching between conductive and non-conductive states is central to the function of ion channels. In potassium channels, inactivation gating occurs by two distinct molecular mechanisms: N-type inactivation (a rapid autoinhibitory process in which an N-terminal particle blocks conduction by binding to the open pore) and C-type inactivation (originating from conformational transitions at the selectivity filter). In the first of two papers, Eduardo Perozo and co-workers solve the X-ray crystal structure of the K+ channel KcsA in an 'open-inactivated' conformation together with a series of crystal structures of channels that are 'trapped' in a set of partially open conformations. In the second paper, the authors identify the underlying mechanism by which movements in the inner gate of this channel trigger conformational changes at the selectivity filter, leading to the non-conductive C-type inactivated state.

Suggested Citation

  • Luis G. Cuello & Vishwanath Jogini & D. Marien Cortes & Albert C. Pan & Dominique G. Gagnon & Olivier Dalmas & Julio F. Cordero-Morales & Sudha Chakrapani & Benoît Roux & Eduardo Perozo, 2010. "Structural basis for the coupling between activation and inactivation gates in K+ channels," Nature, Nature, vol. 466(7303), pages 272-275, July.
    • Handle: RePEc:nat:nature:v:466:y:2010:i:7303:d:10.1038_nature09136
    DOI: 10.1038/nature09136
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    Citations

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    Cited by:

    1. Philipp A. M. Schmidpeter & John T. Petroff & Leila Khajoueinejad & Aboubacar Wague & Cheryl Frankfater & Wayland W. L. Cheng & Crina M. Nimigean & Paul M. Riegelhaupt, 2023. "Membrane phospholipids control gating of the mechanosensitive potassium leak channel TREK1," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Jeroen I Stas & Elke Bocksteins & Alain J Labro & Dirk J Snyders, 2015. "Modulation of Closed−State Inactivation in Kv2.1/Kv6.4 Heterotetramers as Mechanism for 4−AP Induced Potentiation," PLOS ONE, Public Library of Science, vol. 10(10), pages 1-21, October.
    3. Katsumasa Irie & Yoshinori Oda & Takashi Sumikama & Atsunori Oshima & Yoshinori Fujiyoshi, 2023. "The structural basis of divalent cation block in a tetrameric prokaryotic sodium channel," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    4. Tobias Linder & Bert L de Groot & Anna Stary-Weinzinger, 2013. "Probing the Energy Landscape of Activation Gating of the Bacterial Potassium Channel KcsA," PLOS Computational Biology, Public Library of Science, vol. 9(5), pages 1-9, May.
    5. Purushotham Selvakumar & Ana I. Fernández-Mariño & Nandish Khanra & Changhao He & Alice J. Paquette & Bing Wang & Ruiqi Huang & Vaughn V. Smider & William J. Rice & Kenton J. Swartz & Joel R. Meyerson, 2022. "Structures of the T cell potassium channel Kv1.3 with immunoglobulin modulators," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    6. Adam Lewis & Vilius Kurauskas & Marco Tonelli & Katherine Henzler-Wildman, 2021. "Ion-dependent structure, dynamics, and allosteric coupling in a non-selective cation channel," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    7. Ahmed Rohaim & Bram J. A. Vermeulen & Jing Li & Felix Kümmerer & Federico Napoli & Lydia Blachowicz & João Medeiros-Silva & Benoît Roux & Markus Weingarth, 2022. "A distinct mechanism of C-type inactivation in the Kv-like KcsA mutant E71V," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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