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TitleTLR3 forms a laterally aligned multimeric complex along double-stranded RNA for efficient signal transduction.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 164, Year 2023
Publish dateJan 11, 2023
AuthorsKentaro Sakaniwa / Akiko Fujimura / Takuma Shibata / Hideki Shigematsu / Toru Ekimoto / Masaki Yamamoto / Mitsunori Ikeguchi / Kensuke Miyake / Umeharu Ohto / Toshiyuki Shimizu /
PubMed AbstractToll-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 ...Toll-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.
External linksNat Commun / PubMed:36631495 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

EMDB-32599, PDB-7wm4:
Cryo-EM structure of tetrameric TLR3 in complex with dsRNA (90 bp)
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • mus musculus (house mouse)
  • synthetic construct (others)
KeywordsIMMUNE SYSTEM/RNA / innate immunity / IMMUNE SYSTEM / IMMUNE SYSTEM-RNA complex

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