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X-ray structure of a voltage-dependent K+ channel

Author

Listed:
  • Youxing Jiang

    (Rockefeller University
    University of Texas Southwestern Medical Center)

  • Alice Lee

    (Rockefeller University)

  • Jiayun Chen

    (Rockefeller University)

  • Vanessa Ruta

    (Rockefeller University)

  • Martine Cadene

    (Rockefeller University)

  • Brian T. Chait

    (Rockefeller University)

  • Roderick MacKinnon

    (Rockefeller University)

Abstract

Voltage-dependent K+ channels are members of the family of voltage-dependent cation (K+, Na+ and Ca2+) channels that open and allow ion conduction in response to changes in cell membrane voltage. This form of gating underlies the generation of nerve and muscle action potentials, among other processes. Here we present the structure of KvAP, a voltage-dependent K+ channel from Aeropyrum pernix. We have determined a crystal structure of the full-length channel at a resolution of 3.2 Å, and of the isolated voltage-sensor domain at 1.9 Å, both in complex with monoclonal Fab fragments. The channel contains a central ion-conduction pore surrounded by voltage sensors, which form what we call ‘voltage-sensor paddles’—hydrophobic, cationic, helix–turn–helix structures on the channel's outer perimeter. Flexible hinges suggest that the voltage-sensor paddles move in response to membrane voltage changes, carrying their positive charge across the membrane.

Suggested Citation

  • Youxing Jiang & Alice Lee & Jiayun Chen & Vanessa Ruta & Martine Cadene & Brian T. Chait & Roderick MacKinnon, 2003. "X-ray structure of a voltage-dependent K+ channel," Nature, Nature, vol. 423(6935), pages 33-41, May.
    • Handle: RePEc:nat:nature:v:423:y:2003:i:6935:d:10.1038_nature01580
    DOI: 10.1038/nature01580
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    Cited by:

    1. Ozer, Mahmut, 2005. "Determination of rate kinetics in ion channels by the path probability method and Onsager reciprocity theorem," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 357(3), pages 397-414.
    2. Marcos Matamoros & Xue Wen Ng & Joshua B. Brettmann & David W. Piston & Colin G. Nichols, 2023. "Conformational plasticity of NaK2K and TREK2 potassium channel selectivity filters," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Turkan Haliloglu & Nir Ben-Tal, 2008. "Cooperative Transition between Open and Closed Conformations in Potassium Channels," PLOS Computational Biology, Public Library of Science, vol. 4(8), pages 1-11, August.
    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. Spencer C. Guo & Rong Shen & Benoît Roux & Aaron R. Dinner, 2024. "Dynamics of activation in the voltage-sensing domain of Ciona intestinalis phosphatase Ci-VSP," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    6. Jin Wang & Zeyuan Song & Miaolu He & Yongchao Qian & Di Wang & Zheng Cui & Yuan Feng & Shangzhen Li & Bo Huang & Xiangyu Kong & Jinming Han & Lei Wang, 2024. "Light-responsive and ultrapermeable two-dimensional metal-organic framework membrane for efficient ionic energy harvesting," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    7. Shrivastava, Rajan & Malik, Chetan & Ghosh, Subhendu, 2016. "Open channel current noise analysis of S6 peptides from KvAP channel on bilayer lipid membrane shows bimodal power law scaling," Physica A: Statistical Mechanics and its Applications, Elsevier, vol. 451(C), pages 533-540.
    8. Bryan Cernuda & Christopher Thomas Fernandes & Salma Mohamed Allam & Matthew Orzillo & Gabrielle Suppa & Zuleen Chia Chang & Demosthenes Athanasopoulos & Zafir Buraei, 2019. "The molecular determinants of R-roscovitine block of hERG channels," PLOS ONE, Public Library of Science, vol. 14(9), pages 1-26, September.

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