Autor: |
Suno, Ryoji, Sugita, Yukihiko, Morimoto, Kazushi, Takazaki, Hiroko, Tsujimoto, Hirokazu, Hirose, Mika, Suno-Ikeda, Chiyo, Nomura, Norimichi, Hino, Tomoya, Inoue, Asuka, Iwasaki, Kenji, Kato, Takayuki, Iwata, So, Kobayashi, Takuya |
Zdroj: |
Cell Reports; September 2022, Vol. 40 Issue: 11 |
Abstrakt: |
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 E2. Here, we present the single-particle cryoelectron microscopy (cryo-EM) structure of the human EP3-Gisignaling complex at a resolution of 3.4 Å. The structure reveals the binding mode of Gito EP3 and the structural changes induced in EP3 by Gibinding. In addition, we compare the structure of the EP3-Gicomplex with other subtypes of prostaglandin receptors (EP2 and EP4) bound to Gsthat 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. |
Databáze: |
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