Journal article
Architecture of the Neuronal Nicotinic Acetylcholine Receptor Ion Channel at the Binding Site of bis-Ammonium Blockers
Abstract
Abstract. Structure-activity relationships of 56 pentamethylenbis-ammonium compounds, the blockers of the neuronal nicotinic acetylcholine receptor (nAChR) ion channel, have been studied to estimate the cross-sectional dimensions of the channel pore. The cat superior cervical sympathetic ganglion in situ and isolated guinea pig ileum were used to evaluate the potency of the compounds to block ganglionic transmission. Minimum-energy …
Authors
Brovtsyna NB; Tikhonov DB; Gorbunova OB; Gmiro VE; Serduk SE; Lukomskaya NY; Magazanik LG; Zhorov BS
Journal
The Journal of Membrane Biology, Vol. 152, No. 1, pp. 77–87
Publisher
Springer Nature
Publication Date
July 1996
DOI
10.1007/s002329900087
ISSN
0022-2631
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceAnimalsBinding SitesBis-Trimethylammonium CompoundsCatsChickensGuinea PigsIleumIon ChannelsMiceModels, MolecularMolecular Sequence DataNerve Tissue ProteinsProtein ConformationQuaternary Ammonium CompoundsReceptors, NicotinicSerineStructure-Activity RelationshipSuperior Cervical GanglionThreonineTorpedo