6os2 | pdb_00006os2

Structure of synthetic nanobody-stabilized angiotensin II type 1 receptor bound to TRV026

spinqualitylabelsall models 6os2, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6os2 is a 3 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895 and Synthetic construct sequences. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CLR, NAG, OLC NonStd Res: NH2, SAR Gene: AGTR1, AGTR1A, AGTR1B, AT2R1, AT2R1B ("Bacillus coli" Migula 1895) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease [AGTR1_HUMAN] NON RARE IN EUROPE: Essential hypertension;Renal tubular dysgenesis of genetic origin. The disease is caused by mutations affecting the gene represented in this entry. Function [AGTR1_HUMAN] Receptor for angiotensin II. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Publication Abstract from PubMed Biased agonists of G protein-coupled receptors (GPCRs) preferentially activate a subset of downstream signaling pathways. In this work, we present crystal structures of angiotensin II type 1 receptor (AT1R) (2.7 to 2.9 angstroms) bound to three ligands with divergent bias profiles: the balanced endogenous agonist angiotensin II (AngII) and two strongly beta-arrestin-biased analogs. Compared with other ligands, AngII promotes more-substantial rearrangements not only at the bottom of the ligand-binding pocket but also in a key polar network in the receptor core, which forms a sodium-binding site in most GPCRs. Divergences from the family consensus in this region, which appears to act as a biased signaling switch, may predispose the AT1R and certain other GPCRs (such as chemokine receptors) to adopt conformations that are capable of activating beta-arrestin but not heterotrimeric Gq protein signaling. Angiotensin and biased analogs induce structurally distinct active conformations within a GPCR.,Wingler LM, Skiba MA, McMahon C, Staus DP, Kleinhenz ALW, Suomivuori CM, Latorraca NR, Dror RO, Lefkowitz RJ, Kruse AC Science. 2020 Feb 21;367(6480):888-892. doi: 10.1126/science.aay9813. PMID:32079768 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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