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Crystal structure of human glycine receptor-α3 bound to antagonist strychnine

Author

Listed:
  • Xin Huang

    (Amgen Inc.)

  • Hao Chen

    (Amgen Inc.)

  • Klaus Michelsen

    (Amgen Inc.)

  • Stephen Schneider

    (Amgen Inc.)

  • Paul L. Shaffer

    (Amgen Inc.)

Abstract

The X-ray crystal structure of the human glycine receptor in the presence of strychnine, an antagonist, reveals how antagonist binding leads to closure of the channel pore.

Suggested Citation

  • Xin Huang & Hao Chen & Klaus Michelsen & Stephen Schneider & Paul L. Shaffer, 2015. "Crystal structure of human glycine receptor-α3 bound to antagonist strychnine," Nature, Nature, vol. 526(7572), pages 277-280, October.
  • Handle: RePEc:nat:nature:v:526:y:2015:i:7572:d:10.1038_nature14972
    DOI: 10.1038/nature14972
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    Cited by:

    1. Arvind Kumar & Kayla Kindig & Shanlin Rao & Afroditi-Maria Zaki & Sandip Basak & Mark S. P. Sansom & Philip C. Biggin & Sudha Chakrapani, 2022. "Structural basis for cannabinoid-induced potentiation of alpha1-glycine receptors in lipid nanodiscs," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Xiaofen Liu & Weiwei Wang, 2023. "Asymmetric gating of a human hetero-pentameric glycine receptor," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    3. Eric Gibbs & Emily Klemm & David Seiferth & Arvind Kumar & Serban L. Ilca & Philip C. Biggin & Sudha Chakrapani, 2023. "Conformational transitions and allosteric modulation in a heteromeric glycine receptor," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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