7WU9
Cryo-EM structure of the human EP3-Gi signaling complex
Summary for 7WU9
| Entry DOI | 10.2210/pdb7wu9/pdb |
| EMDB information | 32824 |
| Descriptor | Prostaglandin E2 receptor EP3 subtype, Guanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... (5 entities in total) |
| Functional Keywords | gpcr, signal transduction, membrane protein, signaling protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 5 |
| Total formula weight | 149511.54 |
| Authors | Suno, R.,Sugita, Y.,Morimoto, K.,Iwasaki, K.,Kato, T.,Kobayashi, T. (deposition date: 2022-02-07, release date: 2022-08-17, Last modification date: 2024-11-13) |
| Primary citation | Suno, R.,Sugita, Y.,Morimoto, K.,Takazaki, H.,Tsujimoto, H.,Hirose, M.,Suno-Ikeda, C.,Nomura, N.,Hino, T.,Inoue, A.,Iwasaki, K.,Kato, T.,Iwata, S.,Kobayashi, T. Structural insights into the G protein selectivity revealed by the human EP3-G i signaling complex. Cell Rep, 40:111323-111323, 2022 Cited by PubMed Abstract: Prostaglandin receptors have been implicated in a wide range of functions, including inflammation, immune response, reproduction, and cancer. Our group has previously determined the crystal structure of the active-like EP3 bound to its endogenous agonist, prostaglandin E. Here, we present the single-particle cryoelectron microscopy (cryo-EM) structure of the human EP3-G signaling complex at a resolution of 3.4 Å. The structure reveals the binding mode of G to EP3 and the structural changes induced in EP3 by G binding. In addition, we compare the structure of the EP3-G complex with other subtypes of prostaglandin receptors (EP2 and EP4) bound to G that have been previously reported and examine the differences in amino acid composition at the receptor-G protein interface. Mutational analysis reveals that the selectivity of the G protein depends on specific amino acid residues in the second intracellular loop and TM5. PubMed: 36103815DOI: 10.1016/j.celrep.2022.111323 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.375 Å) |
Structure validation
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