Structural insights into the G protein selectivity revealed by the human EP3-Gi signaling complex
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- 寿野, 良二
- Department of Medical Chemistry, Kansai Medical University
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- 杉田, 征彦
- Institute for Protein Research, Osaka University; Hakubi Center for Advanced Research, Kyoto University; Institute for Life and Medical Sciences, Kyoto University
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- 森本, 和志
- Physical Chemistry for Life Science Laboratory, Faculty of Pharmaceutical Sciences, Kyushu University
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- 髙﨑, 寛子
- Institute for Protein Research, Osaka University
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- 辻本, 浩一
- Department of Cell Biology and Medical Chemistry, Graduate School of Medicine, Kyoto University
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- 廣瀬, 未果
- Institute for Protein Research, Osaka University
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- 寿野, 千代
- Department of Medical Chemistry, Kansai Medical University
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- 野村, 紀通
- Department of Cell Biology and Medical Chemistry, Graduate School of Medicine, Kyoto University
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- 日野, 智也
- Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University; Center for Research on Green Sustainable Chemistry, Tottori University
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- 井上, 飛鳥
- Graduate School of Pharmaceutical Sciences, Tohoku University
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- 岩崎, 憲治
- Life Science Center for Survival Dynamics, Tsukuba Advanced Research Alliance (TARA), University of Tsukuba
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- 加藤, 貴之
- Institute for Protein Research, Osaka University
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- 岩田, 想
- Department of Cell Biology and Medical Chemistry, Graduate School of Medicine, Kyoto University
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- 清水(小林), 拓也
- Department of Medical Chemistry, Kansai Medical University; Japan Agency for Medical Research and Development (AMED), Core Research for Evolutional Science and Technology (CREST)
説明
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-Gi signaling complex at a resolution of 3.4 Å. The structure reveals the binding mode of Gi to EP3 and the structural changes induced in EP3 by Gi binding. In addition, we compare the structure of the EP3-Gi complex with other subtypes of prostaglandin receptors (EP2 and EP4) bound to Gs 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.
収録刊行物
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- Cell Reports
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Cell Reports 40 (11), 111323-, 2022-09
Elsevier BV
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キーワード
詳細情報 詳細情報について
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- CRID
- 1050856428650046464
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- ISSN
- 22111247
- 26391856
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- HANDLE
- 2433/276290
- 2324/7161470
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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