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Thermophoretic analysis of ligand-specific conformational states of the inhibitory glycine receptor embedded in copolymer nanodiscs

Bernhard, Max ; Laube, Bodo (2022)
Thermophoretic analysis of ligand-specific conformational states of the inhibitory glycine receptor embedded in copolymer nanodiscs.
In: Scientific Reports, 2022, 10
doi: 10.26083/tuprints-00021126
Artikel, Zweitveröffentlichung, Verlagsversion

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Kurzbeschreibung (Abstract)

The glycine receptor (GlyR), a member of the pentameric ligand-gated ion channel family (pLGIC), displays remarkable variations in the affinity and efficacy of the full agonist glycine and the partial agonist taurine depending on the cell system used. Despite detailed insights in the GlyR three-dimensional structure and activation mechanism, little is known about conformational rearrangements induced by these agonists. Here, we characterized the conformational states of the α1 GlyR upon binding of glycine and taurine by microscale thermophoresis expressed in HEK293 cells and Xenopus oocytes after solubilization in amphipathic styrene-maleic acid copolymer nanodiscs. Our results show that glycine and taurine induce different conformational transitions of the GlyR upon ligand binding. In contrast, the variability of agonist affinity is not mediated by an altered conformational change. Thus, our data shed light on specific agonist induced conformational features and mechanisms of pLGIC upon ligand binding determining receptor activation in native environments.

Typ des Eintrags: Artikel
Erschienen: 2022
Autor(en): Bernhard, Max ; Laube, Bodo
Art des Eintrags: Zweitveröffentlichung
Titel: Thermophoretic analysis of ligand-specific conformational states of the inhibitory glycine receptor embedded in copolymer nanodiscs
Sprache: Englisch
Publikationsjahr: 2022
Publikationsdatum der Erstveröffentlichung: 2022
Verlag: Springer Nature
Titel der Zeitschrift, Zeitung oder Schriftenreihe: Scientific Reports
Jahrgang/Volume einer Zeitschrift: 10
Kollation: 11 Seiten
DOI: 10.26083/tuprints-00021126
URL / URN: https://tuprints.ulb.tu-darmstadt.de/21126
Zugehörige Links:
Herkunft: Zweitveröffentlichung aus gefördertem Golden Open Access
Kurzbeschreibung (Abstract):

The glycine receptor (GlyR), a member of the pentameric ligand-gated ion channel family (pLGIC), displays remarkable variations in the affinity and efficacy of the full agonist glycine and the partial agonist taurine depending on the cell system used. Despite detailed insights in the GlyR three-dimensional structure and activation mechanism, little is known about conformational rearrangements induced by these agonists. Here, we characterized the conformational states of the α1 GlyR upon binding of glycine and taurine by microscale thermophoresis expressed in HEK293 cells and Xenopus oocytes after solubilization in amphipathic styrene-maleic acid copolymer nanodiscs. Our results show that glycine and taurine induce different conformational transitions of the GlyR upon ligand binding. In contrast, the variability of agonist affinity is not mediated by an altered conformational change. Thus, our data shed light on specific agonist induced conformational features and mechanisms of pLGIC upon ligand binding determining receptor activation in native environments.

Status: Verlagsversion
URN: urn:nbn:de:tuda-tuprints-211262
Sachgruppe der Dewey Dezimalklassifikatin (DDC): 500 Naturwissenschaften und Mathematik > 500 Naturwissenschaften
600 Technik, Medizin, angewandte Wissenschaften > 600 Technik
Fachbereich(e)/-gebiet(e): 10 Fachbereich Biologie
10 Fachbereich Biologie > Neurophysiologie und neurosensorische Systeme
Interdisziplinäre Forschungsprojekte
Interdisziplinäre Forschungsprojekte > Centre for Synthetic Biology
Hinterlegungsdatum: 14 Apr 2022 12:12
Letzte Änderung: 19 Apr 2022 05:18
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