5n9b | pdb_00005n9b

Crystal Structure of unliganded human IL-17RA

spinqualitylabelsall models 5n9b, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n9b is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Disease I17RA_HUMAN Defects in IL17RA are the cause of familial candidiasis type 5 (CANDF5) [MIM:613953. CANDF5 is a rare disorder with altered immune responses and impaired clearance of fungal infections, selective against Candida. It is characterized by persistent and/or recurrent infections of the skin, nails and mucous membranes caused by organisms of the genus Candida, mainly Candida albicans. Function I17RA_HUMAN Receptor for IL17A, IL17F and, in dimer with IL17RE, for IL17C. Binds its IL17A ligand with low affinity, suggesting that additional components are involved in IL17A-induced signaling. Publication Abstract from PubMed Signaling through innate immune receptors such as the Toll-like receptor (TLR)/interleukin-1 receptor (IL-1R) superfamily proceeds via the assembly of large membrane-proximal complexes or "signalosomes." Although structurally distinct, the IL-17 receptor family triggers cellular responses that are typical of innate immune receptors. The IL-17RA receptor subunit is shared by several members of the IL-17 family. Using a combination of crystallographic, biophysical, and mutational studies, we show that IL-17A, IL-17F, and IL-17A/F induce IL-17RA dimerization. X-ray analysis of the heteromeric IL-17A complex with the extracellular domains of the IL-17RA and IL-17RC receptors reveals that cytokine-induced IL-17RA dimerization leads to the formation of a 2:2:2 hexameric signaling assembly. Furthermore, we demonstrate that the formation of the IL-17 signalosome potentiates IL-17-induced IL-36gamma and CXCL1 mRNA expression in human keratinocytes, compared with a dimerization-defective IL-17RA variant. IL-17-induced dimerization of IL-17RA drives the formation of the IL-17 signalosome to potentiate signaling.,Goepfert A, Barske C, Lehmann S, Wirth E, Willemsen J, Gudjonsson JE, Ward NL, Sarkar MK, Hemmig R, Kolbinger F, Rondeau JM Cell Rep. 2022 Oct 18;41(3):111489. doi: 10.1016/j.celrep.2022.111489. PMID:36260993 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Interleukin receptor 3D structures

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