7r0j | pdb_00007r0j

Structure of the V2 receptor Cter-arrestin2-ScFv30 complex

spinqualitylabelsall models 7r0j, resolution 4.23Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7r0j is a 3 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.23Å Ligands: SEP, TPO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 beta-arrestin1. It reveals an atypical position of beta-arrestin1 compared to previously described GPCR-arrestin assemblies, associated with an original V2R/beta-arrestin1 interface involving all receptor intracellular loops. Phosphorylated sites of the V2R carboxyl terminus are clearly identified and interact extensively with the beta-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. Structure of the vasopressin hormone-V2 receptor-beta-arrestin1 ternary complex.,Bous J, Fouillen A, Orcel H, Trapani S, Cong X, Fontanel S, Saint-Paul J, Lai-Kee-Him J, Urbach S, Sibille N, Sounier R, Granier S, Mouillac B, Bron P Sci Adv. 2022 Sep 2;8(35):eabo7761. doi: 10.1126/sciadv.abo7761. Epub 2022 Sep 2. PMID:36054364 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Arrestin 3D structures

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