Experimental Physiology
89.2 pp 145-153
DOI: 10.1113/expphysiol.2003.026815
© The Physiological Society 2004
Mechanisms of channel gating of the ligand-gated ion channel superfamily inferred from protein structure
Nathan L. Absalom1,2,
Trevor M. Lewis3 and
Peter R. Schofield1,2
1 Neurobiology Research Program, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia2 School of Medicine, University of New South Wales, St Vincent's Hospital, Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia3 School of Medicine, University of New South Wales, Kensington, NSW, 2052, Australia
The nicotinic-like ligand-gated ion channel superfamily consists of a group of structurally related receptors that activate an ion channel after the binding of extracellular ligand. The recent publications of the crystal structure of an acetylcholine binding protein and a refined electron micrograph structure of the membrane-bound segment of an acetylcholine receptor have led to insights into the molecular determinants of receptor function. Although the structures confirmed much biochemical and electrophysiological data obtained about the receptors, they also provide opportunities to study further the mechanisms that allow channel activation stimulated by ligand-binding. Here we review the mechanisms of channel gating that have been elucidated by information gained from the structures of the acetylcholine binding protein and membrane-bound segment of the acetylcholine receptor.
(Received 30 October 2003;
accepted after revision 13 January 2004)
Corresponding author P. R. Schofield: Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia. Email: p.schofield{at}garvan.org.au
Copyright © 2004 by the The Physiological Society.
