7ylg | pdb_00007ylg

Crystal structure of the chicken Toll-like receptor 15 TIR domain (glutathione adduct)

spinqualitylabelsall models 7ylg, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ylg is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: GSH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H2D5F4_CHICK Cooperates with LY96 to mediate the innate immune response to bacterial lipoproteins and other microbial cell wall components. Cooperates with TLR1 or TLR6 to mediate the innate immune response to bacterial lipoproteins or lipopeptides. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response.[PIRNR:PIRNR037595] Publication Abstract from PubMed Toll-like receptors (TLRs) activate innate immunity in response to pathogen-associated molecular patterns (PAMPs). The ectodomain of a TLR directly senses a PAMP and the intracellular TIR domain dimerizes to initiate a signaling cascade. The TIR domains of TLR6 and TLR10, which belong to the TLR1 subfamily, have been structurally characterized in a dimer, whereas those of other subfamilies, including TLR15, have not been explored at the structural or molecular level. TLR15 is a TLR unique to birds and reptiles that responds to virulence-associated fungal and bacterial proteases. To reveal how the TLR15 TIR domain (TLR15(TIR)) triggers signaling, the crystal structure of TLR15(TIR) was determined in a dimeric form and a mutational study was performed. TLR15(TIR) forms a one-domain structure in which a five-stranded beta-sheet is decorated by alpha-helices, as shown for TLR1 subfamily members. TLR15(TIR) exhibits substantial structural differences from other TLRs at the BB and DD loops and alphaC2 helix that are involved in dimerization. As a result, TLR15(TIR) is likely to form a dimeric structure that is unique in its intersubunit orientation and the contribution of each dimerizing region. Further comparative analysis of TIR structures and sequences provides insights into the recruitment of a signaling adaptor protein by TLR15(TIR). Structural analysis of the Toll-like receptor 15 TIR domain.,Ko KY, Song WS, Park J, Lee GS, Yoon SI IUCrJ. 2023 May 1;10(Pt 3):352-362. doi: 10.1107/S2052252523002956. PMID:37079400 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA