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© Marie Prévost, Institut Pasteur
Image of a portion of a Xenopus oocyte expressing a channel receptor.
Publication : Annual review of pharmacology and toxicology

Nicotinic receptors at the amino acid level

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Annual review of pharmacology and toxicology - 01 Jan 2000

Corringer PJ, Le Novère N, Changeux JP

Link to Pubmed [PMID] – 10836143

Annu. Rev. Pharmacol. Toxicol. 2000;40:431-58

nAChRs are pentameric transmembrane proteins into the superfamily of ligand-gated ion channels that includes the 5HT3, glycine, GABAA, and GABAC receptors. Electron microscopy, affinity labeling, and mutagenesis experiments, together with secondary structure predictions and measurements, suggest an all-beta folding of the N-terminal extracellular domain, with the connecting loops contributing to the ACh binding pocket and to the subunit interfaces that mediate the allosteric transitions between conformational states. The ion channel consists of two distinct elements symmetrically organized along the fivefold axis of the molecule: a barrel of five M2 helices, and on the cytoplasmic side five loops contributing to the selectivity filter. The allosteric transitions of the protein underlying the physiological ACh-evoked activation and desensitization possibly involve rigid body motion of the extracellular domain of each subunit, linked to a global reorganization of the transmembrane domain responsible for channel gating.

http://www.ncbi.nlm.nih.gov/pubmed/10836143