Abstract
The conformations of acetylcholine receptor fromTorpedo californica in the absence and presence of agonists, antagonists, and local anesthetics were studied by circular dichroism (CD). Without ligands, the receptor had about 40% helix, 20% β-sheets, and 10% β-turns as analyzed from its far-UV CD spectrum. Its near-UV CD spectrum resembled that of acetylcholinesterase from the same source. None of the ligands studied altered the far-UV spectrum of the receptor. However, in the near-UV region, carbamylcholine and acetylcholine shifted the Phe and Tyr bands of AChR to less negative, whereas hexamethonium changed the Tyr bands to more negative, indicating that the site of binding of agonists and antagonists and their effect on the conformation of the receptor may be different. Decamethonium, procaine, and lidocaine had no effect on both the far- and near-UV CD spectra of acetylcholine receptor.
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Wu, CS.C., Sun, X.H. & Yang, J.T. Conformation of acetylcholine receptor in the presence of agonists and antagonists. J Protein Chem 9, 119–126 (1990). https://doi.org/10.1007/BF01024993
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DOI: https://doi.org/10.1007/BF01024993