Cellular and Molecular Neurobiology

, Volume 1, Issue 3, pp 231–258

Structural models of the nicotinic acetylcholine receptor and its toxin-binding sites

  • H. Robert Guy

DOI: 10.1007/BF00710680

Cite this article as:
Guy, H.R. Cell Mol Neurobiol (1981) 1: 231. doi:10.1007/BF00710680


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.

Key words

acetylcholine receptor molecular model protein structure snake neurotoxin cholinergic agonists cholinergic antagonists 

Copyright information

© Plenum Publishing Corporation 1981

Authors and Affiliations

  • H. Robert Guy
    • 1
  1. 1.Physiology DepartmentArmed Forces Radiobiology Research InstituteBethesdaUSA
  2. 2.Division of Molecular BiophysicsNINCDS, National Institutes of HealthBethesdaUSA

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