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Hyperekplexia mutations of the glycine receptor unmask the inhibitory subsite for beta-amino-acids.

Laube, Bodo and Langosch, D. and Betz, H. and Schmieden, V. (1995):
Hyperekplexia mutations of the glycine receptor unmask the inhibitory subsite for beta-amino-acids.
In: Neuroreport, pp. 897-900, 6, (6), ISSN 0959-4965, [Article]

Abstract

beta-Alanine and taurine are agonists of the glycine receptor (GlyR) which, at low concentrations, antagonize the action of the principal agonist glycine. We analysed the potency of these ligands on alpha 1 subunits mutated at residue R271. GlyRs formed from alpha 1R271K subunits showed a reduction of beta-alanine and taurine affinities and maximal inducible currents; the mutants alpha 1R271Q and alpha 1R271L associated with human hyperekplexia gave no responses to these ligands. Inhibition of glycine-evoked currents by beta-alanine and taurine, however, was similar for all mutant GlyRs. These data are consistent with the existence of two subdomains within the ligand binding region of the GlyR, an agonistic one, which depends on arginine 271, and an antagonistic subsite, which is not connected to this residue.

Item Type: Article
Erschienen: 1995
Creators: Laube, Bodo and Langosch, D. and Betz, H. and Schmieden, V.
Title: Hyperekplexia mutations of the glycine receptor unmask the inhibitory subsite for beta-amino-acids.
Language: English
Abstract:

beta-Alanine and taurine are agonists of the glycine receptor (GlyR) which, at low concentrations, antagonize the action of the principal agonist glycine. We analysed the potency of these ligands on alpha 1 subunits mutated at residue R271. GlyRs formed from alpha 1R271K subunits showed a reduction of beta-alanine and taurine affinities and maximal inducible currents; the mutants alpha 1R271Q and alpha 1R271L associated with human hyperekplexia gave no responses to these ligands. Inhibition of glycine-evoked currents by beta-alanine and taurine, however, was similar for all mutant GlyRs. These data are consistent with the existence of two subdomains within the ligand binding region of the GlyR, an agonistic one, which depends on arginine 271, and an antagonistic subsite, which is not connected to this residue.

Journal or Publication Title: Neuroreport
Volume: 6
Number: 6
Divisions: 10 Department of Biology
10 Department of Biology > Neurophysiology and Neurosensory Systems
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Date Deposited: 12 Apr 2011 11:18
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