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Title | Structural insights into the G protein selectivity revealed by the human EP3-G signaling complex. |
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Journal, issue, pages | Cell Rep, Vol. 40, Issue 11, Page 111323, Year 2022 |
Publish date | Sep 13, 2022 |
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 / |
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 ...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. |
External links | Cell Rep / PubMed:36103815 |
Methods | EM (single particle) |
Resolution | 3.375 Å |
Structure data | EMDB-32824, PDB-7wu9: |
Source |
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Keywords | SIGNALING PROTEIN / GPCR / signal transduction / MEMBRANE PROTEIN |