Article
An open-channel blocker interacts with adjacent turns of alpha-helices in the nicotinic acetylcholine receptor.
Neuron - 1 Jan 1990
Charnet P, Labarca C, Leonard R J, Vogelaar N J, Czyzyk L, Gouin A, Davidson N, Lester H A
Abstract excerpt
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 electrophysiological analysis. The proposed cytoplasmic end of the M2 transmembrane helix is termed position 1'. At position 1...
Topics
- Amino Acid Sequence
- Amino Acids
- Animals
- Electrophysiology
- Ion Channels
- Kinetics
- Lidocaine
- Mice
- Molecular Sequence Data
- Mutation
- Oocytes
- Protein Conformation
- Receptors, Nicotinic