3CIG
Crystal structure of mouse TLR3 ectodomain
Summary for 3CIG
| Entry DOI | 10.2210/pdb3cig/pdb |
| Related | 3CIY |
| Descriptor | Toll-like receptor 3, 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total) |
| Functional Keywords | leucine-rich repeat, innate immunity, tlr, lrr, glycoprotein, immune response, inflammatory response, membrane, receptor, transmembrane, immune system |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 84591.96 |
| Authors | Liu, L.,Botos, I.,Wang, Y.,Leonard, J.N.,Shiloach, J.,Segal, D.M.,Davies, D.R. (deposition date: 2008-03-11, release date: 2008-05-06, Last modification date: 2024-11-20) |
| Primary citation | Liu, L.,Botos, I.,Wang, Y.,Leonard, J.N.,Shiloach, J.,Segal, D.M.,Davies, D.R. Structural basis of toll-like receptor 3 signaling with double-stranded RNA. Science, 320:379-381, 2008 Cited by PubMed Abstract: Toll-like receptor 3 (TLR3) recognizes double-stranded RNA (dsRNA), a molecular signature of most viruses, and triggers inflammatory responses that prevent viral spread. TLR3 ectodomains (ECDs) dimerize on oligonucleotides of at least 40 to 50 base pairs in length, the minimal length required for signal transduction. To establish the molecular basis for ligand binding and signaling, we determined the crystal structure of a complex between two mouse TLR3-ECDs and dsRNA at 3.4 angstrom resolution. Each TLR3-ECD binds dsRNA at two sites located at opposite ends of the TLR3 horseshoe, and an intermolecular contact between the two TLR3-ECD C-terminal domains coordinates and stabilizes the dimer. This juxtaposition could mediate downstream signaling by dimerizing the cytoplasmic Toll interleukin-1 receptor (TIR) domains. The overall shape of the TLR3-ECD does not change upon binding to dsRNA. PubMed: 18420935DOI: 10.1126/science.1155406 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.66 Å) |
Structure validation
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