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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Autores principales:	J. Niclas Frei, Richard W. Broadhurst, Mark J. Bostock, Andras Solt, Andrew J. Y. Jones, Florian Gabriel, Aditi Tandale, Binesh Shrestha, Daniel Nietlispach
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ac8049b430b14cfaa49fd36fc3a5beb9
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spelling	oai:doaj.org-article:ac8049b430b14cfaa49fd36fc3a5beb92021-12-02T17:32:41ZConformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor10.1038/s41467-020-14526-32041-1723https://doaj.org/article/ac8049b430b14cfaa49fd36fc3a5beb92020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14526-3https://doaj.org/toc/2041-1723The 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.J. Niclas FreiRichard W. BroadhurstMark J. BostockAndras SoltAndrew J. Y. JonesFlorian GabrielAditi TandaleBinesh ShresthaDaniel NietlispachNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
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
title	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_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_sort	conformational plasticity of ligand-bound and ternary gpcr complexes studied by 19f nmr of the β1-adrenergic receptor
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/ac8049b430b14cfaa49fd36fc3a5beb9
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Conformational plasticity of ligand-bound and ternary GPCR complexes studied by 19F NMR of the β1-adrenergic receptor

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