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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. (Publisher's Version)
In: Scientific Reports, 10, Springer Nature, e-ISSN 2045-2322,
DOI: 10.26083/tuprints-00021126,
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Item Type: Article
Origin: Secondary publication via sponsored Golden Open Access
Status: Publisher's Version
Title: Thermophoretic analysis of ligand-specific conformational states of the inhibitory glycine receptor embedded in copolymer nanodiscs
Language: English
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.

Journal or Publication Title: Scientific Reports
Volume of the journal: 10
Place of Publication: Darmstadt
Publisher: Springer Nature
Collation: 11 Seiten
Classification DDC: 500 Naturwissenschaften und Mathematik > 500 Naturwissenschaften
600 Technik, Medizin, angewandte Wissenschaften > 600 Technik
Divisions: 10 Department of Biology > Neurophysiology and Neurosensory Systems
Interdisziplinäre Forschungsprojekte > Centre for Synthetic Biology
Date Deposited: 14 Apr 2022 12:12
Last Modified: 22 Aug 2022 13:20
DOI: 10.26083/tuprints-00021126
Corresponding Links:
URN: urn:nbn:de:tuda-tuprints-211262
URI: https://tuprints.ulb.tu-darmstadt.de/id/eprint/21126
PPN: 494113774
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