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TitlePharmacological modulation of GPR84 revealed by dual states structures and immune functional assays.
Journal, issue, pagesExp Mol Med, Vol. 58, Issue 9, Page 3127-3140, Year 2026
Publish dateSep 10, 2026
AuthorsMyung Kyung Choi / Dong Jin Park / Pankyung Kim / Hee Seong Choi / Sorin Myung / Youngki Yoo / Nienping Chang / Ga-Yeon Yoon / Hye Jin Kang / Sang-Jun Ha / Hyun-Soo Cho /
PubMed AbstractG-protein-coupled receptor 84 (GPR84) is an orphan class A GPCR selectively activated by medium chain fatty acids and highly expressed in immune cells, where it modulates pro-inflammatory signaling. ...G-protein-coupled receptor 84 (GPR84) is an orphan class A GPCR selectively activated by medium chain fatty acids and highly expressed in immune cells, where it modulates pro-inflammatory signaling. The structural basis of GPR84 inactivation and antagonism has remained unclear, limiting the rational design of pathway-selective modulators despite its clinical relevance in metabolic inflammation and fibrotic diseases. Here, we report cryo-electron microscopy structures of human GPR84 in inactive and active states. The 3.5 Å inactive structure bound to the antagonist GLPG1205 reveals a lid-like conformation of extracellular loop 2 and an inward reorientation of Arg172, with the antagonist head group blocking the allosteric sodium-binding site. Molecular dynamics simulations further support these findings, identifying an aberrant TM5, TM6 lateral entry gate. By contrast, the 3.17 Å agonist ZQ-16, Gαi complex, shows a rearranged toggle switch and comparative analyses highlight extracellular loop 2 conformational plasticity. Immune functional assays in THP-1 cells demonstrated that ZQ-16 elicited GPR84-dependent activation and cytokine production, which were effectively abrogated by GLPG1205. Mutagenesis combined with functional assays validates key ligand interactions, providing a framework for the rational design of pathway selective GPR84 modulators.
External linksExp Mol Med / PubMed:42722702 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.5 Å
Structure data

64407

9upy

EMDB-64407, PDB-9upy:
Cryo-EM structure of the ZQ16-bound GPR84 receptor-Gi complex
Method: EM (single particle) / Resolution: 3.1 Å

64807

9v6t

EMDB-64807, PDB-9v6t:
Cryo-EM structure of the GLPG1205-bound GPR84 receptor
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

PDB-1l9k:
dengue methyltransferase

PDB-1l93:
SIMILAR HYDROPHOBIC REPLACEMENTS OF LEU 99 AND PHE 153 WITHIN THE CORE OF T4 LYSOZYME HAVE DIFFERENT STRUCTURAL AND THERMODYNAMIC CONSEQUENCES

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / GPCR / MCFA / complex / agonist / antagonist

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