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TitleStructural basis for lipid-mediated activation of G protein-coupled receptor GPR55.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 1973, Year 2025
Publish dateFeb 25, 2025
AuthorsTobias Claff / Rebecca Ebenhoch / Jörg T Kley / Aniket Magarkar / Herbert Nar / Dietmar Weichert /
PubMed AbstractGPR55 is an orphan G protein-coupled receptor (GPCR) and represents a promising drug target for cancer, inflammation, and metabolic diseases. The endogenous activation of lipid GPCRs can be solely ...GPR55 is an orphan G protein-coupled receptor (GPCR) and represents a promising drug target for cancer, inflammation, and metabolic diseases. The endogenous activation of lipid GPCRs can be solely mediated by membrane components and different lipids have been proposed as endogenous activators of GPR55, such as cannabinoids and lysophosphatidylinositols. Here, we determine high-resolution cryo-electron microscopy structures of the activated GPR55 in complex with heterotrimeric G and two structurally diverse ligands: the putative endogenous agonist 1-palmitoyl-2-lysophosphatidylinositol (LPI) and the synthetic agonist ML184. These results reveal insights into ligand recognition at GPR55, G protein coupling and receptor activation. Notably, an orthosteric binding site opening towards the membrane is observed in both structures, enabling direct interaction of the agonists with membrane lipids. The structural observations are supported by mutagenesis and functional experiments employing G protein dissociation assays. These findings will be of importance for the structure-based development of drugs targeting GPR55.
External linksNat Commun / PubMed:40000629 / PubMed Central
MethodsEM (single particle)
Resolution2.51 - 3.01 Å
Structure data

EMDB-51281: Cryo-EM consensus map of the GPR55-G13-complex bound to synthetic agonist ML184
Method: EM (single particle) / Resolution: 2.64 Å

EMDB-51282: Cryo-EM GPCR focused map of the GPR55-G13-complex bound to synthetic agonist ML184
Method: EM (single particle) / Resolution: 2.77 Å

EMDB-51283: Cryo-EM G protein focused map of the GPR55-G13-complex bound to synthetic agonist ML184
Method: EM (single particle) / Resolution: 2.51 Å

51284

9ge2

EMDB-51284, PDB-9ge2:
Structure of GPR55 in complex with G13 and synthetic agonist ML184
Method: EM (single particle) / Resolution: 2.51 Å

EMDB-51285: Cryo-EM consensus map of the GPR55-G13-complex bound to lysophosphatidylinositol
Method: EM (single particle) / Resolution: 2.96 Å

EMDB-51286: Cryo-EM GPCR focused map of the GPR55-G13-complex bound to lysophosphatidylinositol.
Method: EM (single particle) / Resolution: 3.01 Å

EMDB-51287: Cryo-EM G protein focused map of the GPR55-G13-complex bound to lysophosphatidylinositol
Method: EM (single particle) / Resolution: 2.88 Å

51288

9ge3

EMDB-51288, PDB-9ge3:
Structure of GPR55 in complex with G13 and endogenous lipid agonist lysophosphatidylinositol
Method: EM (single particle) / Resolution: 2.87 Å

Chemicals


PDB Unreleased entry

PDB-1ikh: Unknown entry

ChemComp-CLR:
CHOLESTEROL

ChemComp-HOH:
WATER

PDB-1ikt:
LIGANDED STEROL CARRIER PROTEIN TYPE 2 (SCP-2) LIKE DOMAIN OF HUMAN MULTIFUNCTIONAL ENZYME TYPE 2 (MFE-2)

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
  • aequorea victoria (jellyfish)
KeywordsMEMBRANE PROTEIN / G protein-coupled receptor / GPCR / lipid agonist / cholesterol

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