Structural and functional studies of the nicotinic acetylcholine receptor by solid-state NMR
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Date
2004-05
Publication Type
Conference Paper
ETH Bibliography
yes
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Abstract
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.
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Publication status
published
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Journal / series
Volume
33 (3)
Pages / Article No.
247 - 254
Publisher
Springer
Event
Meeting on Ion Channels - from Biophysics to Disorders
Edition / version
Methods
Software
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Date collected
Date created
Subject
Integral membrane proteins; Magic angle sample spinning; Nicotinic acetylcholine receptor; Oriented samples; Solid-state NMR
Organisational unit
03496 - Meier, Beat H. (emeritus) / Meier, Beat H. (emeritus)
Notes
It was possible to publish this article open access thanks to a Swiss National Licence with the publisher