CaltechAUTHORS
Published April 21, 1995 | Version public
Journal Article Metadata-only

Nicotinic Receptor Binding Site Probed with Unnatural Amino Acid Incorporation in Intact Cells

Creators

Abstract

The nonsense codon suppression method for unnatural amino acid incorporation has been applied to intact cells and combined with electrophysiological analysis to probe structure-function relations in the nicotinic acetylcholine receptor. Functional receptors were expressed in Xenopus oocytes when tyrosine and phenylalanine derivatives were incorporated at positions 93, 190, and 198 in the binding site of the α subunit. Subtle changes in the structure of an individual side chain produced readily detectable changes in the function of this large channel protein. At each position, distinct features of side chain structure dominated the dose-response relation, probably by governing the agonist-receptor binding.

Additional Information

© 1995 American Association for the Advancement of Science. November 1994; accepted 23 January 1995. We thank V. Cornish, P. Deshpande, O. Uhlenbeck, and Y. Zhang for suggestions; E. Chapman for help with synthesis; and J. Jankowski for help with the measurements. Sponsored by grants from NIH, the Office of Naval Research, the Howard Hughes Medical Institute, the University of California Tobacco-Related Disease Research Project, and the Beckman Institute at Caltech.

Additional details

Identifiers

Eprint ID
53893
Resolver ID
CaltechAUTHORS:20150120-140412390

Funding

NIH
Office of Naval Research (ONR)
Howard Hughes Medical Institute (HHMI)
California Tobacco-Related Disease Research Program
Caltech Beckman Institute

Dates

Created
2015-01-21
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Updated
2021-11-10
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