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Structure of nicotinic acetylcholine receptors
Open accessAbstract
Nicotinic acetylcholine (ACh) receptors convert the binding of ACh into the opening of a cation-conducting channel. New information about the regions of the receptor most immediately involved in its function, namely the ACh-binding sites, the gate and the channel, has come from two approaches. One is the identification by labelling and by mutagenesis of residues contributing to these regions. Another is the determination of the three-dimensional structure of the receptor by electron microscopy. Although the identification of functionally relevant residues is incomplete and residues cannot yet be resolved in the three-dimensional structure, the two approaches are converging. There is still room in the gap for speculation.
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Cited by
Cation-π Interactions in Chemistry and Biology: A New View of Benzene, Phe, Tyr, and Trp
Dougherty, D. A. (1996) · Science · doi:10.1126/science.271.5246.163 · Cited by 2,656
Physiological Diversity of Nicotinic Acetylcholine Receptors Expressed by Vertebrate Neurons
McGehee, D. S., & Role, L. W. (1995) · Annual Review of Physiology · doi:10.1146/annurev.ph.57.030195.002513 · Cited by 1,022
The Tetrameric Structure of a Glutamate Receptor Channel
Rosenmund, C., Stern-Bach, Y., & Stevens, C. F. (1998) · Science · doi:10.1126/science.280.5369.1596 · Cited by 794
Miyazawa, A., Fujiyoshi, Y., Stowell, M., & Unwin, N. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2721 · Cited by 490
Functional domains of GABAA receptors
Smith, G. B., & Olsen, R. W. (1995) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)89009-4 · Cited by 489
Metadata
- Authors
- Karlin, A.
- Venue
- Current Opinion in Neurobiology
- Publisher
- Elsevier BV
- Published
- 1993-06
- Volume
- 3
- Issue
- 3
- Pages
- 299-309
- ISSN
- 0959-4388 (ISSN-L)
- OpenAlex
- W2079977484
- Cited by
- 238
- References
- 0
- FWCI
- 2.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
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