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TitleCryo-EM structure of a cell-free synthesized full-length human β1-adrenergic receptor in complex with G.
Journal, issue, pagesStructure, Vol. 33, Issue 11, Page 1867-11877.e5, Year 2025
Publish dateNov 6, 2025
AuthorsFelipe Merino / Zoe Köck / Utz Ermel / Philipp Dahlhaus / Anna Grimm / Anja Seybert / Jan Kubicek / Achilleas S Frangakis / Volker Dötsch / Daniel Hilger / Frank Bernhard /
PubMed AbstractThe 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 ...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 or a G protein mimetic nanobody. To address this, we used cell-free cotranslational insertion of full-length human β1AR into nanodiscs and determined its cryo-electron microscopy (cryo-EM) structure in complex with G. In this structure, ICL3 extends transmembrane helix 5, resulting in enhanced interactions with Gα and in a slight rotation of the engaged G protein. This repositioning enables new polar interactions between Gα, ICL2 and helix 8, while ICL1 and helix 8 form additional contacts with Gβ. These structural insights, supported by mutational analysis, demonstrate that ICL3 enhances G protein activation and downstream cAMP signaling by promoting more extensive interactions between the receptor and the heterotrimeric G protein.
External linksStructure / PubMed:40858117
MethodsEM (single particle)
Resolution3.3 Å
Structure data

19683

8s2t

EMDB-19683, PDB-8s2t:
Cryo-EM structure of cell-free synthesized Human beta-1 adrenergic receptor cotranslationally inserted into a lipidic nanodiscs
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-5FW:
ISOPRENALINE

Source
  • homo sapiens (human)
  • lama glama (llama)
KeywordsMEMBRANE PROTEIN / Signal transduction / GPCR / co-translational nanodisc insertion / G-protein

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