Hauptseite > Publikationsdatenbank > Sub-millisecond conformational dynamics of the A2A adenosine receptor revealed by single-molecule FRET > print

001     1021291
005     20240226075345.0
024 7 _ |a 10.1038/s42003-023-04727-z
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082 _ _ |a 570
100 1 _ |a Maslov, Ivan
|0 0000-0003-3371-4416
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245 _ _ |a Sub-millisecond conformational dynamics of the A2A adenosine receptor revealed by single-molecule FRET
260 _ _ |a London
|c 2023
|b Springer Nature
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500 _ _ |a A.L., A.B., and V.B. are thankful for the Ministry of Science and Higher Education of theRussian Federation (agreement #075-03-2023-106, project FSMG-2020-0003). IMacknowledges the UHasselt Special Research Fund. Measurements of surface expressionand Gs-signaling were supported by the Russian Science Foundation (project no. 22-74-10036; https://rscf.ru/project/22-74-10036/). Computational simulations were supportedby the National Natural Science Foundation of China, grant #32250410316 (to PO). Weacknowledge the Advanced Optical Microscopy Centre at Hasselt University for supportwith microscopy experiments. Microscopy was made possible by the Research Foundation Flanders (FWO, projects G0B4915, G0B9922N, and G0H3716N).
520 _ _ |a The complex pharmacology of G-protein-coupled receptors (GPCRs) is defined by their multi-state conformational dynamics. Single-molecule Förster Resonance Energy Transfer (smFRET) is well suited to quantify dynamics for individual protein molecules; however, its application to GPCRs is challenging. Therefore, smFRET has been limited to studies of inter-receptor interactions in cellular membranes and receptors in detergent environments. Here, we performed smFRET experiments on functionally active human A2A adenosine receptor (A2AAR) molecules embedded in freely diffusing lipid nanodiscs to study their intramolecular conformational dynamics. We propose a dynamic model of A2AAR activation that involves a slow (>2 ms) exchange between the active-like and inactive-like conformations in both apo and antagonist-bound A2AAR, explaining the receptor’s constitutive activity. For the agonist-bound A2AAR, we detected faster (390 ± 80 µs) ligand efficacy-dependent dynamics. Our work establishes a general smFRET platform for GPCR investigations that can potentially be used for drug screening and/or mechanism-of-action studies.
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700 1 _ |a Volkov, Oleksandr
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700 1 _ |a Khorn, Polina
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700 1 _ |a Orekhov, Philipp
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700 1 _ |a Gusach, Anastasiia
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700 1 _ |a Kuzmichev, Pavel
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700 1 _ |a Gerasimov, Andrey
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700 1 _ |a Luginina, Aleksandra
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700 1 _ |a Coucke, Quinten
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700 1 _ |a Bogorodskiy, Andrey
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700 1 _ |a Gordeliy, Valentin
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700 1 _ |a Wanninger, Simon
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700 1 _ |a Barth, Anders
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700 1 _ |a Mishin, Alexey
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700 1 _ |a Hofkens, Johan
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700 1 _ |a Cherezov, Vadim
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700 1 _ |a Gensch, Thomas
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700 1 _ |a Hendrix, Jelle
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700 1 _ |a Borshchevskiy, Valentin
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773 _ _ |a 10.1038/s42003-023-04727-z
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