Article

Cryo-EM structure of a cell-free synthesized full-length human β1-adrenergic receptor in complex with G <sub>s</sub>

2025-04-29

Abstract excerpt

<h4>SUMMARY</h4> The third intracellular loop (ICL3) of the β1-adrenergic receptor (β1AR) plays a critical role in regulating G protein coupling, yet the structural basis has remained unclear due to truncations of ICL3 in all available structures of the β1AR in complex with G s or a G protein mimetic nanobody. To address this, we used cell-free cotranslational insertion of full-length human β1AR into nanodiscs a...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 85229477-1028-5dbd-acb6-c341574ca52d
DOI: 10.1101/2025.04.29.651181

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Cryo-EM structure of a cell-free synthesized full-length human β1-adrenergic receptor in complex with G <sub>s</sub>DOI 10.1101/2025.04.29.651181Read

Cryo-EM structure of the human histamine H1 receptor/Gq complexSemantic proximity Read

Cryo-EM structure of cell-free synthesized human histamine H <sub>2</sub> receptor coupled to heterotrimeric G <sub>s</sub> protein in lipid nanodisc environmentSemantic proximity Read

The CryoEM Structure of Human GPR75: Insights into ECL2-Mediated ActivationSemantic proximity Read

Structural insights into the inactive state of the adhesion GPCR ADGRV1Semantic proximity Read

Cryo-EM complex structure of active GPR75 with a nanobodySemantic proximity Read

Deciphering molecular determinants of GPCR-G protein receptor interactions by complementary integrative structural biology methodsSemantic proximity Read

Refinement of a Cryo-EM Structure of hERG: Bridging Structure and FunctionSemantic proximity Read

Catching the next wave of recombinant RyR2 cryo-EM structures. Commentary on "Molecular basis for gating of cardiac ryanodine receptor explains the mechanisms for gain- and loss-of function mutations".Semantic proximity Read

The hydrophobic amino acid cluster at the cytoplasmic end of transmembrane helix III modulates the coupling of the β(1)-adrenergic receptor to G(s).Semantic proximity Read

Structural and Functional Diversity among Agonist-Bound States of the GLP-1 ReceptorSemantic proximity Read

Domain-interface dynamics of CFTR revealed by stabilizing nanobodiesSemantic proximity Read

Cryo‐EM structure of orphan G protein‐coupled receptor GPR21Semantic proximity Read