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Structure of the carboxy-terminal region of a KCNH channel

Author

Listed:
  • Tinatin I. Brelidze

    (University of Washington School of Medicine, Box 357290, Seattle, Washington 98195-7290, USA)

  • Anne E. Carlson

    (University of Washington School of Medicine, Box 357290, Seattle, Washington 98195-7290, USA)

  • Banumathi Sankaran

    (Berkeley Center for Structural Biology, Lawrence Berkeley National Laboratory, 1 Cyclotron Road, BLDG 6R2100, Berkeley, California 94720, USA)

  • William N. Zagotta

    (University of Washington School of Medicine, Box 357290, Seattle, Washington 98195-7290, USA)

Abstract

The function of the KCNH family of potassium channels is critical for the repolarization of the cardiac action potential and the regulation of neuronal excitability; here, the X-ray crystal structure of the cyclic-nuclotide-binding homology domain of the zebrafish ELK channel is reported.

Suggested Citation

  • Tinatin I. Brelidze & Anne E. Carlson & Banumathi Sankaran & William N. Zagotta, 2012. "Structure of the carboxy-terminal region of a KCNH channel," Nature, Nature, vol. 481(7382), pages 530-533, January.
    • Handle: RePEc:nat:nature:v:481:y:2012:i:7382:d:10.1038_nature10735
    DOI: 10.1038/nature10735
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    Cited by:

    1. Yaming Lu & Miao Yu & Yutian Jia & Fan Yang & Yanming Zhang & Xia Xu & Xiaomin Li & Fan Yang & Jianlin Lei & Yi Wang & Guanghui Yang, 2022. "Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Michael P. Andreas & Tobias W. Giessen, 2024. "The biosynthesis of the odorant 2-methylisoborneol is compartmentalized inside a protein shell," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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