3vbc

Crystal Structure of iL-17 receptor B SEFIR domainCrystal Structure of iL-17 receptor B SEFIR domain

Structural highlights 3vbc is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: Il17rb, Evi27, Il17br (LK3 transgenic mice) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [I17RB_MOUSE] Receptor for the proinflammatory cytokines IL17B and IL17E. May play a role in controlling the growth and/or differentiation of hematopoietic cells. Publication Abstract from PubMed IL-17 cytokines play a crucial role in a variety of inflammatory and autoimmune diseases. They signal through heterodimeric receptor complexes consisting of members of IL-17R family. A unique intracellular signaling domain was identified within all IL-17Rs, termed similar expression to fibroblast growth factor genes and IL-17R (SEFIR). SEFIR is also found in NF-kappaB activator 1 (Act1), an E3 ubiquitin ligase, and mediates its recruitment to IL-17Rs. In this study, to our knowledge, we report the structure of the first SEFIR domain from IL-17RB at 1.8A resolution. SEFIR displays a five-stranded parallel beta-sheet that is wrapped by six helices. Site-directed mutagenesis on IL-17RB identified helix alphaC as being critical for its interaction with Act1 and IL-25 (IL-17E) signaling. Using the current SEFIR structure as a template, the key functional residues in Act1 are also mapped as part of helix alphaC, which is conserved in IL-17RA and RC, suggesting this helix as a common structural signature for heterotypic SEFIR-SEFIR association. In contrast, helix alphaB' is important for homodimerization of Act1, implicating a dual ligand-binding model for SEFIR domain, with distinct structural motifs participating in either homotypic or heterotypic interactions. Furthermore, although the IL-17RB-SEFIR structure resembles closest to the Toll/IL-1R domain of TLR10 with low sequence homology, substantial differences were observed at helices alphaC, alphaD, and DD' loop. To our knowledge, this study provides the first structural view of the IL-17R intracellular signaling, unraveling the mechanism for the specificity of SEFIR versus Toll/IL-1R domain in their respective signaling pathways. Crystal Structure of IL-17 Receptor B SEFIR Domain.,Zhang B, Liu C, Qian W, Han Y, Li X, Deng J J Immunol. 2013 Mar 1;190(5):2320-6. doi: 10.4049/jimmunol.1202922. Epub 2013 Jan, 25. PMID:23355738 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Interleukin receptor

spinqualitylabelsall models 3vbc, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image