7wm4
From Proteopedia
Cryo-EM structure of tetrameric TLR3 in complex with dsRNA (90 bp)
Structural highlights
FunctionTLR3_MOUSE Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response (By similarity).[1] Publication Abstract from PubMedToll-like receptor 3 (TLR3) is a member of the TLR family, which plays an important role in the innate immune system and is responsible for recognizing viral double-stranded RNA (dsRNA). Previous biochemical and structural studies have revealed that a minimum length of approximately 40-50 base pairs of dsRNA is necessary for TLR3 binding and dimerization. However, efficient TLR3 activation requires longer dsRNA and the molecular mechanism underlying its dsRNA length-dependent activation remains unknown. Here, we report cryo-electron microscopy analyses of TLR3 complexed with longer dsRNA. TLR3 dimers laterally form a higher multimeric complex along dsRNA, providing the basis for cooperative binding and efficient signal transduction. TLR3 forms a laterally aligned multimeric complex along double-stranded RNA for efficient signal transduction.,Sakaniwa K, Fujimura A, Shibata T, Shigematsu H, Ekimoto T, Yamamoto M, Ikeguchi M, Miyake K, Ohto U, Shimizu T Nat Commun. 2023 Jan 11;14(1):164. doi: 10.1038/s41467-023-35844-2. PMID:36631495[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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