Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor

The β1-adrenergic receptor (β1AR) is a G-protein-coupled receptor (GPCRs) that binds catecholamine ligands. Here the authors employ site-specific labelling and 19F NMR measurements to characterise the structural changes and dynamics in the cytoplasmic region of β1AR upon agonist stimulation and coup...

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Main Authors: J. Niclas Frei, Richard W. Broadhurst, Mark J. Bostock, Andras Solt, Andrew J. Y. Jones, Florian Gabriel, Aditi Tandale, Binesh Shrestha, Daniel Nietlispach
Format: Article
Language:English
Published: Nature Portfolio 2020-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-14526-3
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author J. Niclas Frei
Richard W. Broadhurst
Mark J. Bostock
Andras Solt
Andrew J. Y. Jones
Florian Gabriel
Aditi Tandale
Binesh Shrestha
Daniel Nietlispach
author_facet J. Niclas Frei
Richard W. Broadhurst
Mark J. Bostock
Andras Solt
Andrew J. Y. Jones
Florian Gabriel
Aditi Tandale
Binesh Shrestha
Daniel Nietlispach
author_sort J. Niclas Frei
collection DOAJ
description The β1-adrenergic receptor (β1AR) is a G-protein-coupled receptor (GPCRs) that binds catecholamine ligands. Here the authors employ site-specific labelling and 19F NMR measurements to characterise the structural changes and dynamics in the cytoplasmic region of β1AR upon agonist stimulation and coupling to a Gs-protein-mimetic nanobody.
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spelling doaj.art-ac8049b430b14cfaa49fd36fc3a5beb92022-12-21T19:32:56ZengNature PortfolioNature Communications2041-17232020-02-0111111410.1038/s41467-020-14526-3Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptorJ. Niclas Frei0Richard W. Broadhurst1Mark J. Bostock2Andras Solt3Andrew J. Y. Jones4Florian Gabriel5Aditi Tandale6Binesh Shrestha7Daniel Nietlispach8Department of Biochemistry, University of CambridgeDepartment of Biochemistry, University of CambridgeDepartment of Biochemistry, University of CambridgeDepartment of Biochemistry, University of CambridgeDepartment of Biochemistry, University of CambridgeDepartment of Biochemistry, University of CambridgeDepartment of Biochemistry, University of CambridgeProtein Sciences, CBT, Novartis Institutes for BioMedical Research (NIBR)Department of Biochemistry, University of CambridgeThe β1-adrenergic receptor (β1AR) is a G-protein-coupled receptor (GPCRs) that binds catecholamine ligands. Here the authors employ site-specific labelling and 19F NMR measurements to characterise the structural changes and dynamics in the cytoplasmic region of β1AR upon agonist stimulation and coupling to a Gs-protein-mimetic nanobody.https://doi.org/10.1038/s41467-020-14526-3
spellingShingle J. Niclas Frei
Richard W. Broadhurst
Mark J. Bostock
Andras Solt
Andrew J. Y. Jones
Florian Gabriel
Aditi Tandale
Binesh Shrestha
Daniel Nietlispach
Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor
Nature Communications
title Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor
title_full Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor
title_fullStr Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor
title_full_unstemmed Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor
title_short Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor
title_sort conformational plasticity of ligand bound and ternary gpcr complexes studied by 19f nmr of the β1 adrenergic receptor
url https://doi.org/10.1038/s41467-020-14526-3
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