5xjm

Complex structure of angiotensin II type 2 receptor with Fab

spinqualitylabelsall models 5xjm, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xjm is a 4 chain structure with sequence from Escherichia coli, Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: SAR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease AGTR2_HUMAN X-linked non-syndromic intellectual disability. Function C562_ECOLX Electron-transport protein of unknown function.AGTR2_HUMAN Receptor for angiotensin II. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation. Publication Abstract from PubMed Angiotensin II (AngII) plays a central role in regulating human blood pressure, which is mainly mediated by interactions between AngII and the G-protein-coupled receptors (GPCRs) AngII type 1 receptor (AT1R) and AngII type 2 receptor (AT2R). We have solved the crystal structure of human AT2R binding the peptide ligand [Sar(1), Ile(8)]AngII and its specific antibody at 3.2-A resolution. [Sar(1), Ile(8)]AngII interacts with both the 'core' binding domain, where the small-molecule ligands of AT1R and AT2R bind, and the 'extended' binding domain, which is equivalent to the allosteric modulator binding site of muscarinic acetylcholine receptor. We generated an antibody fragment to stabilize the extended binding domain that functions as a positive allosteric modulator. We also identified a signature positively charged cluster, which is conserved among peptide-binding receptors, to locate C termini at the bottom of the binding pocket. The reported results should help with designing ligands for angiotensin receptors and possibly to other peptide GPCRs. Crystal structure of the human angiotensin II type 2 receptor bound to an angiotensin II analog.,Asada H, Horita S, Hirata K, Shiroishi M, Shiimura Y, Iwanari H, Hamakubo T, Shimamura T, Nomura N, Kusano-Arai O, Uemura T, Suno C, Kobayashi T, Iwata S Nat Struct Mol Biol. 2018 Jul;25(7):570-576. doi: 10.1038/s41594-018-0079-8. Epub, 2018 Jul 2. PMID:29967536 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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