European Biophysics Journal

, Volume 33, Issue 3, pp 247–254

Structural and functional studies of the nicotinic acetylcholine receptor by solid-state NMR


DOI: 10.1007/s00249-003-0380-1

Cite this article as:
Williamson, P.T.F., Meier, B.H. & Watts, A. Eur Biophys J (2004) 33: 247. doi:10.1007/s00249-003-0380-1


Over the last seven years, solid-state NMR has been widely employed to study structural and functional aspects of the nicotinic acetylcholine receptor. These studies have provided detailed structural information relating to both the ligand binding site and the transmembrane domain of the receptor. Studies of the ligand binding domain have elucidated the nature and the orientation of the pharmacophores responsible for the binding of the agonist acetylcholine within the agonist binding site. Analyses of small transmembrane fragments derived from the nicotinic acetylcholine receptor have also revealed the secondary structure and the orientation of these transmembrane domains. These experiments have expanded our understanding of the channel’s structural properties and are providing an insight into how they might be modulated by the surrounding lipid environment. In this article we review the advances in solid-state NMR applied to the nicotinic acetylcholine receptor and compare the results with recent electron diffraction and X-ray crystallographic studies.


Integral membrane proteinsMagic angle sample spinningNicotinic acetylcholine receptorOriented samplesSolid-state NMR

Copyright information

© EBSA 2004

Authors and Affiliations

  1. 1.Laboratorium für Physikalische ChemieETH-HönggerbergZurichSwitzerland
  2. 2.Biomembrane Structure Unit, Biochemistry DepartmentUniversity of OxfordOxfordUK