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May 30, 2025

Researchers reveal structural basis of prostaglandin D2 receptor DP1 activation and its implications for drug design

The cryo-EM density map of the representative regions of the DP1. Credit: Proceedings of the National Academy of Sciences (2025). DOI: 10.1073/pnas.2501902122
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The cryo-EM density map of the representative regions of the DP1. Credit: Proceedings of the National Academy of Sciences (2025). DOI: 10.1073/pnas.2501902122

Recent breakthroughs in understanding the prostaglandin D2 (PGD2) receptor 1 (DP1) are paving the way for innovative anti-inflammatory and immunomodulatory therapies.

DP1, a G protein-coupled receptor (GPCR), plays a key role in mediating allergic responses and inflammation. Although several DP1-targeting compounds have been identified, their clinical uses have been limited by the lack of detailed molecular understanding.

In a study published in , a research team led by Eric H. Xu (Xu Huaqiang) and Wu Canrong from the Shanghai Institute of Materia Medica (SIMM) of the Chinese Academy of Sciences unveiled high-resolution structures of human DP1.

Using advanced cryo-EM techniques, researchers determined the structures of the DP1 receptor in both its inactive and active states. The active state was resolved in two forms: one in complex with the natural agonist PGD2 and the stimulatory G protein Gs at a resolution of 2.72 Ã…, and the other with the synthetic agonist BW245C and Gs at a resolution of 2.35 Ã…. The inactive state was determined at a resolution of 3.41 Ã….

These structures, combined with functional and mutagenesis studies, revealed unique features of DP1, including an alternative activation mechanism, determinants of ligand selectivity, and characteristics of G protein coupling.

Notably, researchers found that DP1 lacks the conserved W6.48 activation switch and the typical D/ERY motif that is usually involved in GPCR activation, indicating that its activation mechanism is rather unique and not a conserved mechanism.

These molecular insights not only complete the structural framework of PGD2 signaling through its receptor family, but also provide a detailed blueprint for designing selective DP1-targeted drugs—both agonists and antagonists—with greater precision and fewer off-target effects.

This work paves the way for new therapeutic strategies to treat inflammatory and allergic disorders linked to DP1.

More information: Jiuyin Xu et al, Molecular basis for ligand recognition and receptor activation of the prostaglandin D2 receptor DP1, Proceedings of the National Academy of Sciences (2025).

Journal information: Proceedings of the National Academy of Sciences

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High-resolution cryo-EM structures of the human prostaglandin D2 receptor DP1 in both inactive and active states reveal unique activation features, including the absence of the conserved W6.48 switch and D/ERY motif. These findings clarify DP1’s ligand selectivity and G protein coupling, offering a structural basis for designing more selective anti-inflammatory therapies.

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