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-Structure paper
タイトル | Structure of the vasopressin hormone-V2 receptor-β-arrestin1 ternary complex. |
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ジャーナル・号・ページ | Sci Adv, Vol. 8, Issue 35, Page eabo7761, Year 2022 |
掲載日 | 2022年9月2日 |
著者 | Julien Bous / Aurélien Fouillen / Hélène Orcel / Stefano Trapani / Xiaojing Cong / Simon Fontanel / Julie Saint-Paul / Joséphine Lai-Kee-Him / Serge Urbach / Nathalie Sibille / Rémy Sounier / Sébastien Granier / Bernard Mouillac / Patrick Bron / |
PubMed 要旨 | Arrestins interact with G protein-coupled receptors (GPCRs) to stop G protein activation and to initiate key signaling pathways. Recent structural studies shed light on the molecular mechanisms ...Arrestins interact with G protein-coupled receptors (GPCRs) to stop G protein activation and to initiate key signaling pathways. Recent structural studies shed light on the molecular mechanisms involved in GPCR-arrestin coupling, but whether this process is conserved among GPCRs is poorly understood. Here, we report the cryo-electron microscopy active structure of the wild-type arginine-vasopressin V2 receptor (V2R) in complex with β-arrestin1. It reveals an atypical position of β-arrestin1 compared to previously described GPCR-arrestin assemblies, associated with an original V2R/β-arrestin1 interface involving all receptor intracellular loops. Phosphorylated sites of the V2R carboxyl terminus are clearly identified and interact extensively with the β-arrestin1 N-lobe, in agreement with structural data obtained with chimeric or synthetic systems. Overall, these findings highlight a notable structural variability among GPCR-arrestin signaling complexes. |
リンク | Sci Adv / PubMed:36054364 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.23 - 4.73 Å |
構造データ | EMDB-14221, PDB-7r0c: EMDB-14223, PDB-7r0j: |
由来 |
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キーワード | MEMBRANE PROTEIN / G-protein coupled receptor V2 receptor Arrestin 2 Vasopressin |