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Acetylcholine Receptor Channel Structure Probed in Cysteine-Substitution Mutants
Abstract
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—Ser248, Leu250, Ser252, and Thr254—in M2, a membrane-spanning segment of the α subunit, are exposed in the closed channel. Thus α 248-254 probably forms a β strand, and the gate is closer to the cytoplasmic end of the channel than any of these residues. On channel opening, Leu251 is also exposed. These results lead to a revised view of the closed and open channel structures.
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Cited by
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Metadata
- Authors
- Akabas, M. H., Stauffer, D. A., Xu, M., & Karlin, A.
- Venue
- Science
- Published
- 1992-10-09
- Volume
- 258
- Issue
- 5080
- Pages
- 307-310
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1994522080
- Cited by
- 665
- References
- 0
- FWCI
- 12.60
- Type
- journal article
- Language
- en
- Open access
- closed
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- Akabas, M. H., Stauffer, D. A., Xu, M., & Karlin, A. (1992). Acetylcholine Receptor Channel Structure Probed in Cysteine-Substitution Mutants. Science. https://doi.org/10.1126/science.1384130
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