7WM4
Cryo-EM structure of tetrameric TLR3 in complex with dsRNA (90 bp)
Summary for 7WM4
| Entry DOI | 10.2210/pdb7wm4/pdb |
| EMDB information | 32599 |
| Descriptor | Toll-like receptor 3, RNA (81-MER), beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | innate immunity, immune system, immune system-rna complex, immune system/rna |
| Biological source | Mus musculus (house mouse) More |
| Total number of polymer chains | 6 |
| Total formula weight | 377646.32 |
| Authors | Sakaniwa, K.,Ohto, U.,Shimizu, T. (deposition date: 2022-01-14, release date: 2023-01-25, Last modification date: 2025-07-02) |
| Primary citation | Sakaniwa, K.,Fujimura, A.,Shibata, T.,Shigematsu, H.,Ekimoto, T.,Yamamoto, M.,Ikeguchi, M.,Miyake, K.,Ohto, U.,Shimizu, T. TLR3 forms a laterally aligned multimeric complex along double-stranded RNA for efficient signal transduction. Nat Commun, 14:164-164, 2023 Cited by 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 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. PubMed: 36631495DOI: 10.1038/s41467-023-35844-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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