In:
Annual Review of Pharmacology and Toxicology, Annual Reviews, Vol. 40, No. 1 ( 2000-04), p. 431-458
Abstract:
nAChRs are pentameric transmembrane proteins into the superfamily of ligand-gated ion channels that includes the 5HT 3 , glycine, GABA A , and GABA C receptors. Electron microscopy, affinity labeling, and mutagenesis experiments, together with secondary structure predictions and measurements, suggest an all-β 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.
Type of Medium:
Online Resource
ISSN:
0362-1642
,
1545-4304
DOI:
10.1146/pharmtox.2000.40.issue-1
DOI:
10.1146/annurev.pharmtox.40.1.431
Language:
English
Publisher:
Annual Reviews
Publication Date:
2000
detail.hit.zdb_id:
196587-6
detail.hit.zdb_id:
1474461-2
SSG:
15,3
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