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Crystal structure of the α_1B-adrenergic receptor reveals molecular determinants of selective ligand recognition

This study reports the X-ray structure of the α_1B-adrenergic G protein-coupled receptor bound to an inverse agonist, and unveils key determinants of subtype-selective ligand binding that may help the design of aminergic drugs with fewer side-effects.

Mattia Deluigi
Lena Morstein
Andreas Plückthun
ResearchOpen Access19 Jan 2022
Nature Communications

Volume: 13, P: 1-13
Cryo-EM structure of an activated GPCR–G protein complex in lipid nanodiscs

Structures of GPCR neurotensin receptor 1 (NTSR1) in complex with neurotensin and Gα_i1β₁γ₁ in a lipid bilayer environment and without stabilizing antibodies reveal extensive interactions at the GPCR–G protein interface.

Meng Zhang
Miao Gui
Gerhard Wagner
Research25 Feb 2021
Nature Structural & Molecular Biology

Volume: 28, P: 258-267

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Crystal structure of the α1B-adrenergic receptor reveals molecular determinants of selective ligand recognition

Cryo-EM structure of an activated GPCR–G protein complex in lipid nanodiscs

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Crystal structure of the α_1B-adrenergic receptor reveals molecular determinants of selective ligand recognition