3WPF
Crystal structure of mouse TLR9 (unliganded form)
Summary for 3WPF
| Entry DOI | 10.2210/pdb3wpf/pdb |
| Related | 3WPB 3WPC 3WPD 3WPE 3WPG 3WPH 3WPI |
| Descriptor | Toll-like receptor 9, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | leucine rich repeat, receptor, innate immunity, dna binding, glycosylation, dna binding protein |
| Biological source | Mus musculus (mouse) |
| Total number of polymer chains | 1 |
| Total formula weight | 91988.94 |
| Authors | Ohto, U.,Shimizu, T. (deposition date: 2014-01-11, release date: 2015-02-11, Last modification date: 2024-11-13) |
| Primary citation | Ohto, U.,Shibata, T.,Tanji, H.,Ishida, H.,Krayukhina, E.,Uchiyama, S.,Miyake, K.,Shimizu, T. Structural basis of CpG and inhibitory DNA recognition by Toll-like receptor 9 Nature, 520:702-705, 2015 Cited by PubMed Abstract: Innate immunity serves as the first line of defence against invading pathogens such as bacteria and viruses. Toll-like receptors (TLRs) are examples of innate immune receptors, which sense specific molecular patterns from pathogens and activate immune responses. TLR9 recognizes bacterial and viral DNA containing the cytosine-phosphate-guanine (CpG) dideoxynucleotide motif. The molecular basis by which CpG-containing DNA (CpG-DNA) elicits immunostimulatory activity via TLR9 remains to be elucidated. Here we show the crystal structures of three forms of TLR9: unliganded, bound to agonistic CpG-DNA, and bound to inhibitory DNA (iDNA). Agonistic-CpG-DNA-bound TLR9 formed a symmetric TLR9-CpG-DNA complex with 2:2 stoichiometry, whereas iDNA-bound TLR9 was a monomer. CpG-DNA was recognized by both protomers in the dimer, in particular by the amino-terminal fragment (LRRNT-LRR10) from one protomer and the carboxy-terminal fragment (LRR20-LRR22) from the other. The iDNA, which formed a stem-loop structure suitable for binding by intramolecular base pairing, bound to the concave surface from LRR2-LRR10. This structure serves as an important basis for improving our understanding of the functional mechanisms of TLR9. PubMed: 25686612DOI: 10.1038/nature14138 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.959 Å) |
Structure validation
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