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TitleMechanistic insight into signal bias by the agonist-dependent conformational dynamics of GPR84.
Journal, issue, pagesNat Commun, Year 2026
Publish dateJul 16, 2026
AuthorsShota Suzuki / Duy Phuoc Tran / Kouki Nishikawa / Akio Kitao / Yoshinori Fujiyoshi /
PubMed AbstractGPR84 is an orphan class A GPCR primarily expressed in immune cells, where it plays key roles in inflammation and metabolism. Here, we present the cryo-electron microscopy structures of the GPR84-Gi ...GPR84 is an orphan class A GPCR primarily expressed in immune cells, where it plays key roles in inflammation and metabolism. Here, we present the cryo-electron microscopy structures of the GPR84-Gi complex bound to the G protein-biased agonist DL-175, and the inactive state of GPR84 bound to the antagonist GLPG1205. Combined with signaling assays and molecular dynamics simulations, these structures elucidate the conformational landscape spanning the inactive and G protein-biased active states of GPR84, providing a mechanistic basis for biased agonism. Notably, steric interactions between DL-175 and L336 selectively preclude the conformational changes required for efficient β-arrestin recruitment without compromising G protein activation. These structural insights provide a structural context for the rational design of GPR84-targeted therapeutics with precisely tuned signaling profiles.
External linksNat Commun / PubMed:42463693
MethodsEM (single particle)
Resolution3.05 - 3.43 Å
Structure data

65995

9wij

EMDB-65995, PDB-9wij:
Cryo-EM structure of GPR84 with GLPG1205
Method: EM (single particle) / Resolution: 3.05 Å

EMDB-65996: Cryo-EM structure of GPR84-Gi with DL-175 (foucus receptor)
Method: EM (single particle) / Resolution: 3.43 Å

EMDB-65997: Cryo-EM structure of GPR84-Gi complex with DL-175 (Gi focus)
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-65998: Cryo-EM structure of GPR84-Gi complex with DL-175 (Consensus)
Method: EM (single particle) / Resolution: 3.3 Å

65999

9wik

EMDB-65999, PDB-9wik:
Cryo-EM structure of GPR84-Gi complex with DL-175
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

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


PDB Unreleased entry

PDB-1mbr: Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
  • escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / GPCR / SIGNALING PROTEIN

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