{"systematicName":"2XLY96:2XTLR4","synonyms":["TLR4/MD-2 complex"],"functions":["Type I membrane receptor that plays a crucial role in innate immunity by recognizing conserved patterns in diverse microbial molecules including lipoproteins, lipopeptides, lipopolysaccharide, flagellin, and nucleic acids. In the early step of bacterial infection, serum lipopolysaccharide (LPS, CHEBI:16412) binds to the N-terminal of LBP (P18428), LPS is then presented to CD14 (P08571) and transferred to LY96 or the LY96-TLR4 toll-like receptor complex. This induces the dimerization of TLR4 TIR domains, initiating CD14-dependent TLR4 endocytosis, and TICAM1/TRIF(Q8IUC6)-dependent signal transduction to promote inflammation caused by LPS."],"properties":["LY96 is a soluble glycoprotein with a sandwich structure of two anti-parallel beta-sheets which lack disulfide bonds, enabling a change in the antiparallel beta-sheets spatial configuration on binding TLR4 to build a bulky internal pocket, which allows the LY96-TLR4 complex to bind to LPS. Ligand binding causes the TLR molecules to reorient their TIR domains (IPR000157), which allow docking of TIR containing proteins, such as MYD88 (Q99836) through TIR-TIR interactions. 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