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Structure and gating mechanism of the acetylcholine receptor pore

Author

Listed:
  • Atsuo Miyazawa

    (RIKEN Harima Institute)

  • Yoshinori Fujiyoshi

    (Kyoto University)

  • Nigel Unwin

    (MRC Laboratory of Molecular Biology)

Abstract

The nicotinic acetylcholine receptor controls electrical signalling between nerve and muscle cells by opening and closing a gated, membrane-spanning pore. Here we present an atomic model of the closed pore, obtained by electron microscopy of crystalline postsynaptic membranes. The pore is shaped by an inner ring of 5 α-helices, which curve radially to create a tapering path for the ions, and an outer ring of 15 α-helices, which coil around each other and shield the inner ring from the lipids. The gate is a constricting hydrophobic girdle at the middle of the lipid bilayer, formed by weak interactions between neighbouring inner helices. When acetylcholine enters the ligand-binding domain, it triggers rotations of the protein chains on opposite sides of the entrance to the pore. These rotations are communicated through the inner helices, and open the pore by breaking the girdle apart.

Suggested Citation

  • Atsuo Miyazawa & Yoshinori Fujiyoshi & Nigel Unwin, 2003. "Structure and gating mechanism of the acetylcholine receptor pore," Nature, Nature, vol. 423(6943), pages 949-955, June.
    • Handle: RePEc:nat:nature:v:423:y:2003:i:6943:d:10.1038_nature01748
    DOI: 10.1038/nature01748
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    Cited by:

    1. Eva Chovancova & Antonin Pavelka & Petr Benes & Ondrej Strnad & Jan Brezovsky & Barbora Kozlikova & Artur Gora & Vilem Sustr & Martin Klvana & Petr Medek & Lada Biedermannova & Jiri Sochor & Jiri Damb, 2012. "CAVER 3.0: A Tool for the Analysis of Transport Pathways in Dynamic Protein Structures," PLOS Computational Biology, Public Library of Science, vol. 8(10), pages 1-12, October.
    2. Arthur A. Melo & Thiemo Sprink & Jeffrey K. Noel & Elena Vázquez-Sarandeses & Chris Hoorn & Saif Mohd & Justus Loerke & Christian M. T. Spahn & Oliver Daumke, 2022. "Cryo-electron tomography reveals structural insights into the membrane remodeling mode of dynamin-like EHD filaments," Nature Communications, Nature, vol. 13(1), pages 1-13, 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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