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Amino acids of the Torpedo marmorata acetylcholine receptor .alpha. subunit labeled by a photoaffinity ligand for the acetylcholine binding site
Abstract
The acetylcholine-binding sites on the native, membrane-bound acetylcholine receptor from Torpedo marmorata were covalently labeled with the photoaffinity reagent [3H]-p-(dimethylamino)-benzenediazonium fluoroborate (DDF) in the presence of phencyclidine by employing an energy-transfer photolysis procedure. The alpha-chains isolated from receptor-rich membranes photolabeled in the absence or presence of carbamoylcholine were cleaved with CNBr and the radiolabeled fragments purified by high-performance liquid chromatography. Amino acid and/or sequence analysis demonstrated that the alpha-chain residues Trp-149, Tyr-190, Cys-192, and Cys-193 and an unidentified residue(s) in the segment alpha 31-105 were all labeled by the photoaffinity reagent in an agonist-protectable manner. The labeled amino acids are located within three distinct regions of the large amino-terminal hydrophilic domain of the alpha-subunit primary structure and plausibly lie in proximity to one another at the level of the acetylcholine-binding sites in the native receptor. These findings are in accord with models proposed for the transmembrane topology of the alpha-chain that assign the amino-terminal segment alpha 1-210 to the synaptic cleft. Furthermore, the results suggest that the four identified [3H]DDF-labeled residues, which are conserved in muscle and neuronal alpha-chains but not in the other subunits, may be directly involved in agonist binding.
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Metadata
- Authors
- Dennis, M., Giraudat, J., Kotzyba-Hibert, F., Goeldner, M., Hirth, C., Chang, J. Y., Lazure, C., Chretien, M., & Changeux, J. P.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1988-04-05
- Volume
- 27
- Issue
- 7
- Pages
- 2346-2357
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2010244456
- Cited by
- 317
- References
- 38
- FWCI
- 9.40
- Type
- journal article
- Language
- en
- Open access
- closed
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