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In pursuit of the high‐resolution structure of nicotinic acetylcholine receptors
Author(s) -
Chen Lin
Publication year - 2010
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2009.184085
Subject(s) - nicotinic agonist , acetylcholine receptor , acetylcholine , nicotinic acetylcholine receptor , mechanism (biology) , neuroscience , drug discovery , function (biology) , high resolution , receptor , chemistry , computational biology , biology , bioinformatics , pharmacology , microbiology and biotechnology , biochemistry , physics , remote sensing , quantum mechanics , geology
The nicotinic acetylcholine receptor (nAChR) has been studied extensively for well over four decades because of its important physiological roles and medical relevance. A large body of data from biochemical and biophysical studies are now available. The structural information, which is needed to integrate existing data to address the mechanism and function of nAChRs, started to emerge in recent years. Structural studies of acetylcholine binding proteins (AChBPs) have greatly facilitated the study of nAChRs. The recently determined crystal structures of the prokaryotic homologues of nAChRs will probably have similar impact over time. However, a direct structural model of nAChRs at high resolution will be important for mechanistic studies and drug development. Here we will review some of the recent efforts in this area and use the high‐resolution structure of the extracellular domains of nAChR α1 to illustrate the potential insights one may gain at higher resolution.