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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Nature Portfolio
2020-02-01
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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. |
first_indexed | 2024-12-20T16:45:36Z |
format | Article |
id | doaj.art-ac8049b430b14cfaa49fd36fc3a5beb9 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-20T16:45:36Z |
publishDate | 2020-02-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
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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