An open-channel blocker interacts with adjacent turns of α-helices in the nicotinic acetylcholine receptor

• Published in: Neuron (Cambridge, Mass.) Vol. 4; no. 1; pp. 87 - 95
• Main Authors: Charnet, Pierre, Labarca, Cesar, Leonard, Reid J., Vogelaar, Nancy J., Czyzyk, Linda, Gouin, Annie, Davidson, Norman, Lester, Henry A.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 1990
• Subjects: Amino Acid Sequence; Amino Acids - metabolism; Animals; Electrophysiology; Ion Channels - metabolism; Kinetics; Lidocaine - analogs & derivatives; Lidocaine - metabolism; Lidocaine - pharmacology; Mice; Molecular Sequence Data; Mutation; Oocytes; Protein Conformation; Receptors, Nicotinic - drug effects

The binding site for an open-channel blocker, QX-222, at mouse muscle nicotinic acetylcholine receptors was probed using site-directed mutagenesis, oocyte expression, and elect rophysiologicaI analysis. The proposed cytoplasmic end of the M2 transmembrane helix is termed position 1′. At position 10′...