The selectivity filter of a ligand-gated ion channel. The helix-M2 model of the ion channel of the nicotinic acetylcholine receptor

Ferdinand Hucho; Rolf Hilgenfeld

doi:10.1016/0014-5793(89)81775-2

The selectivity filter of a ligand-gated ion channel. The helix-M2 model of the ion channel of the nicotinic acetylcholine receptor

Ferdinand Hucho^*, Rolf Hilgenfeld

^*Corresponding author for this work

Institute of Biochemistry

Freie Universität Berlin

37 Citations (Scopus)

Abstract

Evidence from electrophysiology and biochemistry supports the hypothesis that the ion channel of the nicotinic acetylcholine receptor is formed by homologous amino acid sequences of all receptor subunits, called helices M2. A model of the ion channel is proposed and the selectivity filter is described as a ring of negatively-charged amino acid side chains [(1988) Nature 335, 645-648] which may undergo conformational changes upon permeation of the cation. Acetylcholine receptor; Ion channel; Selectivity filter; Molecular modeling.

Original language	English
Journal	FEBS Letters
Volume	257
Issue number	1
Pages (from-to)	17-23
Number of pages	7
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(89)81775-2
Publication status	Published - 23.10.1989

Funding

Acknowledgements: Work by one of the authors, (F.H.), referred to in this article was supported by the Deutsche Forschungsgemeinschaft (SFB 312) and the Fonds der Chemischen Industrie.

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Academic Focus: Center for Infection and Inflammation Research (ZIEL)

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10.1016/0014-5793(89)81775-2

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abstract = "Evidence from electrophysiology and biochemistry supports the hypothesis that the ion channel of the nicotinic acetylcholine receptor is formed by homologous amino acid sequences of all receptor subunits, called helices M2. A model of the ion channel is proposed and the selectivity filter is described as a ring of negatively-charged amino acid side chains [(1988) Nature 335, 645-648] which may undergo conformational changes upon permeation of the cation. Acetylcholine receptor; Ion channel; Selectivity filter; Molecular modeling.",

author = "Ferdinand Hucho and Rolf Hilgenfeld",

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AU - Hucho, Ferdinand

AU - Hilgenfeld, Rolf

N1 - Funding Information: Acknowledgements: Work by one of the authors, (F.H.), referred to in this article was supported by the Deutsche Forschungsgemeinschaft (SFB 312) and the Fonds der Chemischen Industrie. Copyright: Copyright 2014 Elsevier B.V., All rights reserved.

PY - 1989/10/23

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N2 - Evidence from electrophysiology and biochemistry supports the hypothesis that the ion channel of the nicotinic acetylcholine receptor is formed by homologous amino acid sequences of all receptor subunits, called helices M2. A model of the ion channel is proposed and the selectivity filter is described as a ring of negatively-charged amino acid side chains [(1988) Nature 335, 645-648] which may undergo conformational changes upon permeation of the cation. Acetylcholine receptor; Ion channel; Selectivity filter; Molecular modeling.

AB - Evidence from electrophysiology and biochemistry supports the hypothesis that the ion channel of the nicotinic acetylcholine receptor is formed by homologous amino acid sequences of all receptor subunits, called helices M2. A model of the ion channel is proposed and the selectivity filter is described as a ring of negatively-charged amino acid side chains [(1988) Nature 335, 645-648] which may undergo conformational changes upon permeation of the cation. Acetylcholine receptor; Ion channel; Selectivity filter; Molecular modeling.

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The selectivity filter of a ligand-gated ion channel. The helix-M2 model of the ion channel of the nicotinic acetylcholine receptor

Abstract

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