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A structural model for the ligand‐binding sites at the nicotinic acetylcholine receptor
Author(s) -
Smart Louis,
Meyers Hans-Wilhelm,
Hilgenfeld Rolf,
Saenger Wolfram,
Maelicke Alfred
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81241-7
Subject(s) - torpedo , acetylcholine receptor , nicotinic acetylcholine receptor , peptide , chemistry , residue (chemistry) , cholinergic , nicotinic agonist , binding site , biophysics , receptor , biochemistry , acetylcholine , ligand (biochemistry) , stereochemistry , biology , neuroscience , pharmacology
The structural properties of a selected segment of the 4 polypeptide chains of the acetylcholine receptor from Torpedo californica have been compared by model building studies. The particular segment (residues 135–142) is identical for the β, γ and δ subunits but differs in one position from the otherwise identical α‐peptide. We conclude that the exchange of a tryptophanyl by a glutaminyl residue may produce a sufficiently different folding and charge pattern to provide for the specific binding of cholinergic ligands to the α‐peptide.