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The structural mechanism of KCNH-channel regulation by the eag domain

Author

Listed:
  • Yoni Haitin

    (University of Washington School of Medicine)

  • Anne E. Carlson

    (University of Washington School of Medicine)

  • William N. Zagotta

    (University of Washington School of Medicine)

Abstract

An X-ray crystal structure of two intracellular domains of a mouse KCNH voltage-dependent potassium channel, EAG1, is presented: the structure reveals that the eag domain interacts directly with the cyclic nucleotide-binding homology domain (CNBHD), and that many KCNH-associated disease mutations are localized to the eag domain–CNBHD interface.

Suggested Citation

  • Yoni Haitin & Anne E. Carlson & William N. Zagotta, 2013. "The structural mechanism of KCNH-channel regulation by the eag domain," Nature, Nature, vol. 501(7467), pages 444-448, September.
    • Handle: RePEc:nat:nature:v:501:y:2013:i:7467:d:10.1038_nature12487
    DOI: 10.1038/nature12487
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    Cited by:

    1. Ting-Feng Lin & Guey-Mei Jow & Hsin-Yu Fang & Ssu-Ju Fu & Hao-Han Wu & Mei-Miao Chiu & Chung-Jiuan Jeng, 2014. "The Eag Domain Regulates the Voltage-Dependent Inactivation of Rat Eag1 K+ Channels," PLOS ONE, Public Library of Science, vol. 9(10), pages 1-14, October.
    2. 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.

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