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TitleMolecular insights into ligand recognition and receptor activation of GPR15.
Journal, issue, pagesiScience, Vol. 28, Issue 12, Page 113935, Year 2025
Publish dateDec 19, 2025
AuthorsShutian Chen / Xuteng Han / Yuxia Zhang / Limin Ma / Cuiying Yi / Xiaojing Chu / Qiuxiang Tan / Shuo Han / Qiang Zhao / Beili Wu /
PubMed AbstractIn response to the chemokine-like peptide GPR15L, G protein-coupled receptor 15 (GPR15) is crucial for immune cell trafficking and inflammatory diseases. However, understanding of its physiology and ...In response to the chemokine-like peptide GPR15L, G protein-coupled receptor 15 (GPR15) is crucial for immune cell trafficking and inflammatory diseases. However, understanding of its physiology and pathology is hindered by lack of molecular details of the interaction between GPR15 and the full-length GPR15L. Here, we report the structure of GPR15 bound to the full-length GPR15L and G protein. Combined with mutagenesis data, this structure reveals key interactions that define ligand recognition and a subpocket that governs GPR15L selectivity and receptor activation. Molecular dynamics simulations suggest that sulfation modifications in the N-terminal region of GPR15 may play a role in stabilizing the binding between GPR15 and the core region of GPR15L. Furthermore, molecular docking of some potential small-molecule antagonists suggests a conserved molecular pattern of these ligands inhibiting receptor activation. These findings provide essential insight into functional modulation of GPR15 and would facilitate development of therapeutic strategies for treatment of inflammation and immune diseases.
External linksiScience / PubMed:41321630 / PubMed Central
MethodsEM (single particle)
Resolution3.05 - 3.3 Å
Structure data

EMDB-65823: Overall cryo-EM map of GPR15
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-65824: Focused cryo-EM map of GPR15 transmembrane domain
Method: EM (single particle) / Resolution: 3.05 Å

66350

9wxm

EMDB-66350, PDB-9wxm:
Cryo-EM structure of the full-length GPR15L bound GPR15-Gi complex
Method: EM (single particle) / Resolution: 3.3 Å

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN/IMMUNE SYSTEM / GPCR / GPR15L / GPR15 / MEMBRANE PROTEIN-IMMUNE SYSTEM complex

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