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Structure of the Acetylcholine-Gated Channel

  1. Gregory Bock Organizer,
  2. Jamie A. Goode
  1. Nigel Unwin

Published Online: 7 OCT 2008

DOI: 10.1002/0470868759.ch2

Ion Channels: From Atomic Resolution Physiology to Functional Genomics: Novartis Foundation Symposium 245

Ion Channels: From Atomic Resolution Physiology to Functional Genomics: Novartis Foundation Symposium 245

How to Cite

Unwin, N. (2008) Structure of the Acetylcholine-Gated Channel, in Ion Channels: From Atomic Resolution Physiology to Functional Genomics: Novartis Foundation Symposium 245 (eds G. Bock and J. A. Goode), John Wiley & Sons, Ltd, Chichester, UK. doi: 10.1002/0470868759.ch2

Author Information

  1. MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK

Publication History

  1. Published Online: 7 OCT 2008
  2. Published Print: 19 APR 2002

Book Series:

  1. Novartis Foundation Symposia

Book Series Editors:

  1. Novartis Foundation

ISBN Information

Print ISBN: 9780470843758

Online ISBN: 9780470868751

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Summary

The structure of the acetylcholine-gated channel, trapped in open as well as closed states, has been analysed by electron crystallographic methods. The channel has large vestibules extending from the membrane which shape the acetylcholine-binding pockets and facilitate selective transport of cations across a narrow membrane-spanning pore. When acetylcholine enters these pockets it triggers a concerted conformational change that opens the pore by destabilizing a gate in the middle of the membrane made by a ring of pore-lining α-helical segments. The alternative ‘open’ configuration of pore-lining segments reshapes the lumen and creates new surfaces, allowing the ions to pass through. Recent results, at nearly 4 Å resolution, have defined more precisely the structure of the pore and the design of the vestibular entrances.