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-Structure paper
Title | TLR3 forms a laterally aligned multimeric complex along double-stranded RNA for efficient signal transduction. |
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Journal, issue, pages | Nat Commun, Vol. 14, Issue 1, Page 164, Year 2023 |
Publish date | Jan 11, 2023 |
Authors | Kentaro Sakaniwa / Akiko Fujimura / Takuma Shibata / Hideki Shigematsu / Toru Ekimoto / Masaki Yamamoto / Mitsunori Ikeguchi / Kensuke Miyake / Umeharu Ohto / Toshiyuki Shimizu / |
PubMed Abstract | 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 ...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 links | Nat Commun / PubMed:36631495 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.2 Å |
Structure data | EMDB-32599, PDB-7wm4: |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | IMMUNE SYSTEM/RNA / innate immunity / IMMUNE SYSTEM / IMMUNE SYSTEM-RNA complex |