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Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic

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Abstract

Introduction by site-directed mutagenesis of three amino acids from the Mil segment of glycine or & GAMMA;-aminobutyric acid (GABAA) receptors into the Mil segment of α7 nicotinic receptor was sufficient to convert a cation-selective channel into an an ion-selective channel gated by acetylcholine. A critical mutation was the insertion of an uncharged residue at the amino-terminal end of Mil, stressing the importance of protein geometrical constraints on ion selectivity.

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Authors and Affiliations

  1. Neurobiologie Moléculaire, Unité de Recherche Associée au Centre National de la Recherche Scientifique D1284, Institut Pasteur, 25 rue du Dr Roux, 75724, Paris, Cedex 15, France

    Jean-Luc Galzi, Anne Devillers-Thiery & Jean-Pierre Changeux

  2. Département de Physiologie, Centre Médical Universitaire (Faculté de Médecine), 1211, Geneva, 4, Switzerland

    Nicolas Hussy, Sonia Bertrand & Daniel Bertrand

Authors
  1. Jean-Luc Galzi
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  2. Anne Devillers-Thiery
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  3. Nicolas Hussy
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  4. Sonia Bertrand
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  5. Jean-Pierre Changeux
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  6. Daniel Bertrand
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Galzi, JL., Devillers-Thiery, A., Hussy, N. et al. Mutations in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to anionic. Nature 359, 500–505 (1992). https://doi.org/10.1038/359500a0

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