Abstract
Models of the protein structure of agonist-, competitive antagonist-, and snake neurotoxin-binding sites were designed using the sequence of the first 54 residues of the acetylcholine receptor (AChR)α subunit from Torpedo californica. These models are based on the premise that the N-terminal portions of the subunits form the outermost extracellular surface of the AChR and that agonists bind to this portion. The models were developed by predicting the secondary strucutre of theα-subunit N-terminal segment from its sequence, then using these predictions to fold the segment into tertiary structures that should bind snake neurotoxins, agonists, and antagonists. Possible gating mechanisms and quaternary structures are suggested by the proposed tertiary structures of the subunits. Experiments are suggested to test aspects of the models.
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Supported by Armed Forces Radiobiology Research Institute, Defense Nuclear Agency, under Research Work Unit MJ 00032. The views presented in this paper are those of the author. No endorsement by the Defense Nuclear Agency has been given or should be inferred.
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Guy, H.R. Structural models of the nicotinic acetylcholine receptor and its toxin-binding sites. Cell Mol Neurobiol 1, 231–258 (1981). https://doi.org/10.1007/BF00710680
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DOI: https://doi.org/10.1007/BF00710680