Acetylcholine Receptor Channel Structure Probed in Cysteine-Substitution Mutants

In order to understand the structural bases of ion conduction, ion selectivity, and gating in the nicotinic acetylcholine receptor, mutagenesis and covalent modification were combined to identify the amino acid residues that line the channel. The side chains of alternate residues-Ser$^{248}$, Leu$^{...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1992-10, Vol.258 (5080), p.307-310
Hauptverfasser:	Akabas, Myles H., Stauffer, David A., Xu, Ming, Karlin, Arthur
Format:	Artikel
Sprache:	eng
Schlagworte:	Acetylcholine Acetylcholine - metabolism Acetylcholine - pharmacology Acetylcholine receptors Agonists Amino Acid Sequence Amino acids Animals Biological and medical sciences Cell receptors Cell structures and functions channels Cholinergic receptors cysteine Cysteine - chemistry Fundamental and applied biological sciences. Psychology Gene Expression Ion Channel Gating Ion Channels - chemistry Ion Channels - physiology Messenger RNA Mice Molecular and cellular biology Molecular Sequence Data Monoamines receptors (catecholamine, serotonine, histamine, acetylcholine) Muscles - chemistry Mutagenesis mutants Nicotinic receptors Oocytes Oocytes - metabolism Physicians Physiology probes Protein structure Proteins Reagents Receptors Receptors, Cholinergic - chemistry Receptors, Cholinergic - genetics Structure Structure-Activity Relationship substitutions Sulfhydryl Reagents - pharmacology Surgeons Thermodynamics Transfection Xenopus
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