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Evidence for Multipoint Attachment of Ligands to the Nicotinic Acetylcholine Receptor

  • Alfred Maelicke
  • Gregor Fels
  • Bianca M. Conti-Tronconi
Conference paper
Part of the NATO ASI Series book series (volume 32)

Abstract

Binding of 125I-labelled α-bungarotoxin (αBTX) and of several 3H-labelled αBTX-competitive anti-nAChR antibodies suggest that the cholinergic binding site(s) are “discontinuous”, i.e. they are formed by several sequence segments which are well separated along the primary structure of the nAChR α-subunit (Conti-Tronconi et al., 1989). Presumably, these non-continuous segments are brought together, by the tertiary folding of the α-subunit, to form the area of the nAChR surface recognized by the neurotoxin and the antibodies. Our data agree with previous reports (Neumann et al., 1986; Gotti et al., 1987; Ralston et al., 1987; Gershoni 1987; Gotti et al., 1989; Gershoni et al., 1989) in that the region around cysteines 192 and 193 forms a major component of the toxin binding site. They result in a different model of the cholinergic binding site, however, in that they suggest a rather intricately structured binding region, with particular sensitivity to con-formational changes and the capability of selective binding of classes of ligands (Conti-Tronconi et al., unpublished).

Keywords

Acetylcholine Receptor Nicotinic Acetylcholine Receptor Nicotinic Cholinergic Receptor Sequence Portion Acetylcholine Recep 
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 1989

Authors and Affiliations

  • Alfred Maelicke
    • 1
  • Gregor Fels
    • 1
  • Bianca M. Conti-Tronconi
    • 2
  1. 1.Max-Planck-Institut für ErnährungsphysiologieDortmund 1Germany
  2. 2.Department of BiochemistryUniversity of MinnesotaSt. PaulUSA

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