ArticleNature chemical biology2019
Ligand binding to human prostaglandin E receptor EP
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Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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53citing papers in PubMed
9.2field-weighted citation impact, top 1% of its field
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Who cites it
53 citing papers in PubMed, 114 citations in OpenAlex.
- Structural analysis of rhodopsin states in megabody complexes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Diuretic and Anti-hyperuricemic Effects of Geranyl Acetate in Rats.Current medicinal chemistry · 2026Article
- Structural insights into selective and dual antagonism of EP2 and EP4 prostaglandin receptors.The EMBO journal · 2025Article
- Structural insights into the mechanism of activation and inhibition of the prostaglandin D2 receptor 1.Nature communications · 2025Article
- Structural insights into the activation of the human prostaglandin EProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Instruction multi-constraint molecular generation using a teacher-student large language model.BMC biology · 2025Article
- Article
- Antibodies expand the scope of angiotensin receptor pharmacology.Nature chemical biology · 2024Article
- Spinster homolog 2/S1P signaling ameliorates macrophage inflammatory response to bacterial infections by balancing PGECell communication and signaling : CCS · 2024Article
- G Protein-Coupled Receptor-Ligand Pose and Functional Class Prediction.International journal of molecular sciences · 2024Article
- Controlling spatial distribution of functional lipids in a supported lipid bilayer prepared from vesicles.Journal of colloid and interface science · 2024Article
- Structures of human prostaglandin FNature communications · 2023Article
- Docking for EP4R antagonists active against inflammatory pain.Nature communications · 2023Article
- Structural basis of antibody inhibition and chemokine activation of the human CC chemokine receptor 8.Nature communications · 2023Article
- Single hormone or synthetic agonist induces GProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural basis of αNature communications · 2023Article
- Discovery of Novel, Selective Prostaglandin EP4 Receptor Antagonists with Efficacy in Cancer Models.ACS medicinal chemistry letters · 2023Article
- Drug repurposing screens to identify potential drugs for chronic kidney disease by targeting prostaglandin E2 receptor.Computational and structural biotechnology journal · 2023Article
- A robust antibody discovery platform for difficult-to-express G protein-coupled receptors.Protein science : a publication of the Protein Society · 2023Article
- Structural basis for recognition of antihistamine drug by human histamine receptor.Nature communications · 2022Article
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Authors and funding
33 authors at 11 institutions in 2 countries.
Yosuke ToyodaDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.ORCID http://orcid.org/0000-0002-2245-4666
Kazushi MorimotoDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.ORCID http://orcid.org/0000-0001-7698-9378
Ryoji SunoDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.
Shoichiro HoritaDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.
Keitaro YamashitaRIKEN SPring-8 Center, Sayo-cho, Sayo-gun, Hyogo, Japan.ORCID http://orcid.org/0000-0002-5442-7582
Kunio HirataRIKEN SPring-8 Center, Sayo-cho, Sayo-gun, Hyogo, Japan.
Yusuke SekiguchiDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.
Satoshi YasudaDepartment of Chemistry, Graduate School of Science, Chiba University, Inage, Chiba, Japan.ORCID http://orcid.org/0000-0003-3555-1083
Mitsunori ShiroishiGraduate School of Pharmaceutical Sciences, Kyushu University, Higashi-ku, Fukuoka, Japan.
Tomoko ShimizuNB Health Laboratory Co. Ltd., Kita Ward Sapporo City, Hokkaido, Japan.
Yuji UrushibataNB Health Laboratory Co. Ltd., Kita Ward Sapporo City, Hokkaido, Japan.
Yuta KajiwaraGraduate School of Energy Science, Kyoto University, Uji, Kyoto, Japan.
Tomoaki InazumiDepartment of Pharmaceutical Biochemistry, Graduate School of Pharmaceutical Sciences, Kumamoto University, Oe-Honmachi, Kumamoto, Japan.
Yunhon HottaDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.ORCID http://orcid.org/0000-0003-4062-1103
Hidetsugu AsadaDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.ORCID http://orcid.org/0000-0001-6255-4728
Takanori NakaneDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.ORCID http://orcid.org/0000-0003-2697-2767
Yuki ShiimuraDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.
Tomoya NakagitaDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.ORCID http://orcid.org/0000-0002-0542-8650
Kyoshiro TsugeDepartment of Pharmaceutical Biochemistry, Graduate School of Pharmaceutical Sciences, Kumamoto University, Oe-Honmachi, Kumamoto, Japan.ORCID http://orcid.org/0000-0001-9419-7331
Suguru YoshidaLaboratory of Chemical Bioscience, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, Chiyoda-ku, Tokyo, Japan.ORCID http://orcid.org/0000-0001-5888-9330
Tomoko KuribaraLaboratory of Chemical Bioscience, Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, Chiyoda-ku, Tokyo, Japan.
Takamitsu HosoyaJapan Science and Technology Agency (JST), Platform for Drug Discovery, Informatics, and Structural Life Science, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.ORCID http://orcid.org/0000-0002-7270-351X
Yukihiko SugimotoDepartment of Pharmaceutical Biochemistry, Graduate School of Pharmaceutical Sciences, Kumamoto University, Oe-Honmachi, Kumamoto, Japan.ORCID http://orcid.org/0000-0001-6973-932X
Norimichi NomuraDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.ORCID http://orcid.org/0000-0002-6330-2239
Miwa SatoBiomedical Department, Mitsui Knowledge Industry Co., Minato-ku, Tokyo, Japan.
Takatsugu HirokawaJapan Science and Technology Agency (JST), Platform for Drug Discovery, Informatics, and Structural Life Science, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan.
Masahiro KinoshitaInstitute of Advanced Energy, Kyoto University, Uji, Kyoto, Japan.ORCID http://orcid.org/0000-0001-8060-045X
Takeshi MurataDepartment of Chemistry, Graduate School of Science, Chiba University, Inage, Chiba, Japan.ORCID http://orcid.org/0000-0002-5748-4670
Kiyoshi TakayamaNB Health Laboratory Co. Ltd., Kita Ward Sapporo City, Hokkaido, Japan.
Masaki YamamotoRIKEN SPring-8 Center, Sayo-cho, Sayo-gun, Hyogo, Japan.
Shuh NarumiyaJapan Agency for Medical Research and Development (AMED), Core Research for Evolutional Science and Technology (CREST), Chiyoda-ku, Tokyo, Japan. s.naru@mfour.med.kyoto-u.ac.jp.
So IwataDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan. s.iwata@mfour.med.kyoto-u.ac.jp.ORCID http://orcid.org/0000-0003-1735-2937
Takuya KobayashiDepartment of Medical Chemistry and Cell Biology, Kyoto University Graduate School of Medicine, Konoe-cho, Yoshida, Sakyo-ku, Kyoto, Japan. kobayashi.takuya.4r@kyoto-u.ac.jp.
Kyoto University · JPTokyo Medical and Dental University · JPChiba University · JPKumamoto University · JPSPring-8 · JPJapan Agency for Medical Research and Development · JPJapan Science and Technology Agency · JPKyushu University · JPMitsui (Japan) · JPObayashi (Japan) · JPUniversity of Tsukuba · JP
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prostaglandin E receptor EP4, a G-protein-coupled receptor, is involved in disorders such as cancer and autoimmune disease. Here, we report the crystal structure of human EP4 in complex with its antagonist ONO-AE3-208 and an inhibitory antibody at 3.2 Å resolution. The structure reveals that the extracellular surface is occluded by the extracellular loops and that the antagonist lies at the interface with the lipid bilayer, proximal to the highly conserved Arg316 residue in the seventh transmembrane domain. Functional and docking studies demonstrate that the natural agonist PGE
Indexed as
Allosteric RegulationAnimalsAntibodies, MonoclonalBinding SitesCaprylatesCrystallography, X-RayEpoprostenolHumansLigandsLipid BilayersMolecular Docking SimulationNaphthalenesPhenylbutyratesPhenyl EthersReceptors, Prostaglandin E, EP4 SubtypeSpodoptera4-(4-cyano-2-(2-(4-fluoronaphthalen-1-yl)propionylamino)phenyl)butyric acidAGN 34 compoundAntibodies, MonoclonalCaprylatesEpoprostenolKAG-308LigandsLipid BilayersNaphthalenesPhenylbutyratesPhenyl EthersPTGER4 protein, humanReceptors, Prostaglandin E, EP4 Subtype
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.