7WU9

Cryo-EM structure of the human EP3-Gi signaling complex

7WU9 の概要

• エントリーDOI: 10.2210/pdb7wu9/pdb
• EMDBエントリー: 32824
• 分子名称: 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)
• 機能のキーワード: gpcr, signal transduction, membrane protein, signaling protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 149511.54

構造登録者

Suno, R.,Sugita, Y.,Morimoto, K.,Iwasaki, K.,Kato, T.,Kobayashi, T. (登録日: 2022-02-07, 公開日: 2022-08-17, 最終更新日: 2024-11-13)

主引用文献

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

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: 36103815
DOI: 10.1016/j.celrep.2022.111323

実験手法

ELECTRON MICROSCOPY (3.375 Å)