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Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry.

Kuhse, J. ; Laube, Bodo ; Magalei, D. ; Betz, H. (1993)
Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry.
In: Neuron, 11 (6)
Article, Bibliographie

Abstract

The inhibitory glycine receptor (GlyR) is a pentameric protein composed of two types (alpha and beta) of membrane-spanning subunits. Coexpression in Xenopus oocytes of a low affinity mutant of the alpha 2 subunit with the alpha 1 and beta subunits indicated that GlyRs assembled from alpha 1 and alpha 2 polypeptides contain variable subunit ratios, whereas alpha/beta hetero-oligomers have an invariant (3:2) stoichiometry. Analysis of different alpha/beta chimeric constructs revealed that this difference in assembly behavior is mediated by the N-terminal extracellular regions of the receptor subunits. Substitution of residues diverging between the alpha and beta subunits identified combinations of sequence motifs determining subunit stoichiometry.

Item Type: Article
Erschienen: 1993
Creators: Kuhse, J. ; Laube, Bodo ; Magalei, D. ; Betz, H.
Type of entry: Bibliographie
Title: Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry.
Language: English
Date: 1993
Journal or Publication Title: Neuron
Volume of the journal: 11
Issue Number: 6
Abstract:

The inhibitory glycine receptor (GlyR) is a pentameric protein composed of two types (alpha and beta) of membrane-spanning subunits. Coexpression in Xenopus oocytes of a low affinity mutant of the alpha 2 subunit with the alpha 1 and beta subunits indicated that GlyRs assembled from alpha 1 and alpha 2 polypeptides contain variable subunit ratios, whereas alpha/beta hetero-oligomers have an invariant (3:2) stoichiometry. Analysis of different alpha/beta chimeric constructs revealed that this difference in assembly behavior is mediated by the N-terminal extracellular regions of the receptor subunits. Substitution of residues diverging between the alpha and beta subunits identified combinations of sequence motifs determining subunit stoichiometry.

Divisions: 10 Department of Biology
10 Department of Biology > Neurophysiology and Neurosensory Systems
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Date Deposited: 12 Apr 2011 11:27
Last Modified: 05 Mar 2019 06:48
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