7r0c

Structure of the AVP-V2R-arrestin2-ScFv30 complex

spinqualitylabelsall models 7r0c, resolution 4.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7r0c is a 4 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 4.73Å Ligands: NH2, SEP, TPO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease V2R_HUMAN Nephrogenic syndrome of inappropriate antidiuresis;Inappropriate antidiuretic hormone secretion syndrome;Nephrogenic diabetes insipidus. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. Function V2R_HUMAN Receptor for arginine vasopressin. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Involved in renal water reabsorption. 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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