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
22 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 languageEnglish
JournalFEBS Letters
Volume178
Issue number1
Pages (from-to)64-68
Number of pages5
ISSN0014-5793
DOIs
Publication statusPublished - 03.12.1984

Research Areas and Centers

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

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