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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)
Artikel, Bibliographie

Kurzbeschreibung (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.

Typ des Eintrags: Artikel
Erschienen: 1993
Autor(en): Kuhse, J. ; Laube, Bodo ; Magalei, D. ; Betz, H.
Art des Eintrags: Bibliographie
Titel: Assembly of the inhibitory glycine receptor: identification of amino acid sequence motifs governing subunit stoichiometry.
Sprache: Englisch
Publikationsjahr: 1993
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Neuron
Jahrgang/Volume einer Zeitschrift: 11
(Heft-)Nummer: 6
Kurzbeschreibung (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.

Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Neurophysiologie und neurosensorische Systeme
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Hinterlegungsdatum: 12 Apr 2011 11:27
Letzte Änderung: 05 Mär 2019 06:48
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