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

J. Niclas Frei; Richard W. Broadhurst; Mark J. Bostock; Andras Solt; Andrew J. Y. Jones; Florian Gabriel; Aditi Tandale; Binesh Shrestha; Daniel Nietlispach

doi:10.1038/s41467-020-14526-3

Nature Communications (Feb 2020)

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

J. Niclas Frei,
Richard W. Broadhurst,
Mark J. Bostock,
Andras Solt,
Andrew J. Y. Jones,
Florian Gabriel,
Aditi Tandale,
Binesh Shrestha,
Daniel Nietlispach

Affiliations

J. Niclas Frei: Department of Biochemistry, University of Cambridge
Richard W. Broadhurst: Department of Biochemistry, University of Cambridge
Mark J. Bostock: Department of Biochemistry, University of Cambridge
Andras Solt: Department of Biochemistry, University of Cambridge
Andrew J. Y. Jones: Department of Biochemistry, University of Cambridge
Florian Gabriel: Department of Biochemistry, University of Cambridge
Aditi Tandale: Department of Biochemistry, University of Cambridge
Binesh Shrestha: Protein Sciences, CBT, Novartis Institutes for BioMedical Research (NIBR)
Daniel Nietlispach: Department of Biochemistry, University of Cambridge

DOI: https://doi.org/10.1038/s41467-020-14526-3
Journal volume & issue: Vol. 11, no. 1
pp. 1 – 14

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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