A structural model for the ligand-binding sites at the nicotinic acetylcholine receptor

Louis Smart; Hans Wilhelm Meyers; Rolf Hilgenfeld; Wolfram Saenger; Alfred Maelicke

doi:10.1016/0014-5793(84)81241-7

A structural model for the ligand-binding sites at the nicotinic acetylcholine receptor

Louis Smart, Hans Wilhelm Meyers, Rolf Hilgenfeld, Wolfram Saenger, Alfred Maelicke^*

^*Corresponding author for this work

Institute of Biochemistry

23 Citations (Scopus)

Abstract

The structural properties of a selected segment of the 4 polypeptide chains of the acetylcholine receptor from Torpedo californica have been compared by model building studies. The particular segment (residues 135-142) is identical for the β, γ and δ subunits but differs in one position from the otherwise identical α-peptide. We conclude that the exchange of a tryptophanyl by a glutaminyl residue may produce a sufficiently different folding and charge pattern to provide for the specific binding of cholinergic ligands to the α-peptide.

Original language	English
Journal	FEBS Letters
Volume	178
Issue number	1
Pages (from-to)	64-68
Number of pages	5
ISSN	0014-5793
DOIs	https://doi.org/10.1016/0014-5793(84)81241-7
Publication status	Published - 03.12.1984

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

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10.1016/0014-5793(84)81241-7

Cite this

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abstract = "The structural properties of a selected segment of the 4 polypeptide chains of the acetylcholine receptor from Torpedo californica have been compared by model building studies. The particular segment (residues 135-142) is identical for the β, γ and δ subunits but differs in one position from the otherwise identical α-peptide. We conclude that the exchange of a tryptophanyl by a glutaminyl residue may produce a sufficiently different folding and charge pattern to provide for the specific binding of cholinergic ligands to the α-peptide.",

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AU - Meyers, Hans Wilhelm

AU - Hilgenfeld, Rolf

AU - Saenger, Wolfram

AU - Maelicke, Alfred

PY - 1984/12/3

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AB - The structural properties of a selected segment of the 4 polypeptide chains of the acetylcholine receptor from Torpedo californica have been compared by model building studies. The particular segment (residues 135-142) is identical for the β, γ and δ subunits but differs in one position from the otherwise identical α-peptide. We conclude that the exchange of a tryptophanyl by a glutaminyl residue may produce a sufficiently different folding and charge pattern to provide for the specific binding of cholinergic ligands to the α-peptide.

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A structural model for the ligand-binding sites at the nicotinic acetylcholine receptor

Abstract

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