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

^*Korrespondierende/r Autor/-in für diese Arbeit

Institut für Biochemie

Freie Universität Berlin

37 Zitate (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.

Originalsprache	Englisch
Zeitschrift	FEBS Letters
Jahrgang	257
Ausgabenummer	1
Seiten (von - bis)	17-23
Seitenumfang	7
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(89)81775-2
Publikationsstatus	Veröffentlicht - 23.10.1989

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

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",

note = "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.",

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doi = "10.1016/0014-5793(89)81775-2",

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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

Y1 - 1989/10/23

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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DO - 10.1016/0014-5793(89)81775-2

M3 - Journal articles

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IS - 1

ER -

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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