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A Structural Model of the Ion Channel of the Nicotinic Acetylcholine Receptor

  • F. Hucho
  • W. Oberthür
  • F. Lottspeich
  • B. Wittmann-Liebold
Conference paper
Part of the NATO ASI Series book series (volume 3)

Abstract

The nicotinic acetylcholine receptor (nAChR) consists operationally of two functional parts: the signal recognition (acetylcholine binding) site and the ion channel. Both are integral parts of the heteropentameric receptor protein and appear not to be separable as molecular entities. Their interaction has been described in analogy to other allosteric proteins (1) as mediated by conformational changes of the protein conveyed from the ligand binding sites to the gating mechanism of the channel.

Keywords

Tryptic Peptide Nicotinic Acetylcholine Receptor Molecular Entity Edman Degradation Cyanogen Bromide 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1986

Authors and Affiliations

  • F. Hucho
    • 1
  • W. Oberthür
    • 1
  • F. Lottspeich
    • 2
  • B. Wittmann-Liebold
    • 3
  1. 1.Institut für Biochemie, Arbeitsgruppe NeurochemieFreie Universität BerlinBerlin 33Germany
  2. 2.Max-Planck-Institut für BiochemieMartinsriedGermany
  3. 3.Max-Planck-Institut für Molekulare Genetik, Abteilung WittmannBerlin 33Germany

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