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Structural basis for inhibition of a voltage-gated Ca2+ channel by Ca2+ antagonist drugs

Author

Listed:
  • Lin Tang

    (University of Washington
    Howard Hughes Medical Institute, University of Washington)

  • Tamer M. Gamal El-Din

    (University of Washington)

  • Teresa M. Swanson

    (University of Washington)

  • David C. Pryde

    (Curadev Pharma)

  • Todd Scheuer

    (University of Washington)

  • Ning Zheng

    (University of Washington
    Howard Hughes Medical Institute, University of Washington)

  • William A. Catterall

    (University of Washington)

Abstract

Calcium channel blockers are widely used to treat cardiovascular diseases; new structural studies uncover how two different types of calcium-channel blockers bind to the channel; the drugs bind in different locations, revealing different mechanisms of drug action.

Suggested Citation

  • Lin Tang & Tamer M. Gamal El-Din & Teresa M. Swanson & David C. Pryde & Todd Scheuer & Ning Zheng & William A. Catterall, 2016. "Structural basis for inhibition of a voltage-gated Ca2+ channel by Ca2+ antagonist drugs," Nature, Nature, vol. 537(7618), pages 117-121, September.
    • Handle: RePEc:nat:nature:v:537:y:2016:i:7618:d:10.1038_nature19102
    DOI: 10.1038/nature19102
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    Cited by:

    1. Gamma Chi & Qiansheng Liang & Akshay Sridhar & John B. Cowgill & Kasim Sader & Mazdak Radjainia & Pu Qian & Pablo Castro-Hartmann & Shayla Venkaya & Nanki Kaur Singh & Gavin McKinley & Alejandra Ferna, 2022. "Cryo-EM structure of the human Kv3.1 channel reveals gating control by the cytoplasmic T1 domain," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Yiqing Wei & Zhuoya Yu & Lili Wang & Xiaojing Li & Na Li & Qinru Bai & Yuhang Wang & Renjie Li & Yufei Meng & Hao Xu & Xianping Wang & Yanli Dong & Zhuo Huang & Xuejun Cai Zhang & Yan Zhao, 2024. "Structural bases of inhibitory mechanism of CaV1.2 channel inhibitors," Nature Communications, Nature, vol. 15(1), pages 1-11, December.

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