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Recent advances in understanding the structure of nicotinic acetylcholine receptors
Author(s) -
Zouridakis Marios,
Zisimopoulou Paraskevi,
Poulas Konstantinos,
Tzartos Socrates J.
Publication year - 2009
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.170
Subject(s) - nicotinic agonist , acetylcholine receptor , cys loop receptors , acetylcholine , nicotinic acetylcholine receptor , ligand gated ion channel , ion channel , neuromuscular junction , microbiology and biotechnology , protein subunit , neuroscience , receptor , biology , torpedo , chemistry , biophysics , biochemistry , pharmacology , gene
Nicotinic acetylcholine receptors (nAChRs), members of the Cys‐loop ligand‐gated ion channels (LGICs) superfamily, are involved in signal transduction upon binding of the neurotransmitter acetylcholine or exogenous ligands, such as nicotine. nAChRs are pentameric assemblies of homologous subunits surrounding a central pore that gates cation flux, and are expressed at the neuromuscular junction and in the nervous system and several nonneuronal cell types. The 17 known nAChR subunits assemble into a variety of pharmacologically distinct receptor subtypes. nAChRs are implicated in a range of physiological functions and pathophysiological conditions related to muscle contraction, learning and memory, reward, motor control, arousal, and analgesia, and therefore present an important target for drug research. Such studies would be greatly facilitated by knowledge of the high‐resolution structure of the nAChR. Although this information is far from complete, important progress has been made mainly based on electron microscopy studies of Torpedo nAChR and the high‐resolution X‐ray crystal structures of the homologous molluscan acetylcholine‐binding proteins, the extracellular domain of the mouse nAChR α1 subunit, and two prokaryotic pentameric LGICs. Here, we review some of the latest advances in our understanding of nAChR structure and gating. © 2009 IUBMB IUBMB Life, 61(4): 407–423, 2009