6AK3
Crystal structure of the human prostaglandin E receptor EP3 bound to prostaglandin E2
Summary for 6AK3
| Entry DOI | 10.2210/pdb6ak3/pdb |
| Descriptor | Prostaglandin E2 receptor EP3 subtype,Soluble cytochrome b562, (Z)-7-[(1R,2R,3R)-3-hydroxy-2-[(E,3S)-3-hydroxyoct-1-enyl]-5-oxo-cyclopentyl]hept-5-enoic acid, (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate (3 entities in total) |
| Functional Keywords | gpcr, lipid, signaling protein, prostanoid receptor, membrane protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 94314.50 |
| Authors | Morimoto, K.,Suno, R.,Iwata, S.,Kobayashi, T. (deposition date: 2018-08-29, release date: 2018-12-05, Last modification date: 2024-11-06) |
| Primary citation | Morimoto, K.,Suno, R.,Hotta, Y.,Yamashita, K.,Hirata, K.,Yamamoto, M.,Narumiya, S.,Iwata, S.,Kobayashi, T. Crystal structure of the endogenous agonist-bound prostanoid receptor EP3. Nat. Chem. Biol., 15:8-10, 2019 Cited by PubMed Abstract: Prostanoids are a series of bioactive lipid metabolites that function in an autacoid manner via activation of cognate G-protein-coupled receptors (GPCRs). Here, we report the crystal structure of human prostaglandin (PG) E receptor subtype EP3 bound to endogenous ligand PGE at 2.90 Å resolution. The structure reveals important insights into the activation mechanism of prostanoid receptors and provides a molecular basis for the binding modes of endogenous ligands. PubMed: 30510192DOI: 10.1038/s41589-018-0171-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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