Japan Agency for Medical Research and Development (AMED)
JP21am0101072 (support number 1113), JP19am0101115 (support number 2365)
Japan
Japan Agency for Medical Research and Development (AMED)
JP21gm0910007
Japan
Japan Agency for Medical Research and Development (AMED)
JP21am0401020
Japan
Japan Society for the Promotion of Science (JSPS)
15K08268, 19H03428,20H03434
Japan
Ministry of Education, Culture, Sports, Science and Technology (Japan)
21H05112
Japan
Japan Agency for Medical Research and Development (AMED)
JP20ak010110
Japan
Citation
Journal: Cell Rep / Year: 2022 Title: Structural insights into the G protein selectivity revealed by the human EP3-G signaling complex. Authors: Ryoji Suno / Yukihiko Sugita / Kazushi Morimoto / Hiroko Takazaki / Hirokazu Tsujimoto / Mika Hirose / Chiyo Suno-Ikeda / Norimichi Nomura / Tomoya Hino / Asuka Inoue / Kenji Iwasaki / ...Authors: Ryoji Suno / Yukihiko Sugita / Kazushi Morimoto / Hiroko Takazaki / Hirokazu Tsujimoto / Mika Hirose / Chiyo Suno-Ikeda / Norimichi Nomura / Tomoya Hino / Asuka Inoue / Kenji Iwasaki / Takayuki Kato / So Iwata / Takuya Kobayashi / 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 ...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.
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