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- EMDB-32599: Cryo-EM structure of tetrameric TLR3 in complex with dsRNA (90 bp) -
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Open data
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Basic information
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Title | Cryo-EM structure of tetrameric TLR3 in complex with dsRNA (90 bp) | ||||||||||||
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Function / homology | ![]() type III interferon production / positive regulation of type III interferon production / response to dsRNA / regulation of dendritic cell cytokine production / inflammatory response to wounding / toll-like receptor 3 signaling pathway / necroptotic signaling pathway / positive regulation of cytokine production involved in inflammatory response / positive regulation of macrophage cytokine production / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Sakaniwa K / Ohto U | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: TLR3 forms a laterally aligned multimeric complex along double-stranded RNA for efficient signal transduction. Authors: Kentaro Sakaniwa / Akiko Fujimura / Takuma Shibata / Hideki Shigematsu / Toru Ekimoto / Masaki Yamamoto / Mitsunori Ikeguchi / Kensuke Miyake / Umeharu Ohto / Toshiyuki Shimizu / ![]() 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. | ||||||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 41.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 12.5 KB 12.5 KB | Display Display | ![]() |
Images | ![]() | 61.5 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7wm4MC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1.128 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Tetrameric TLR3 in complex with dsRNA (90 bp)
Entire | Name: Tetrameric TLR3 in complex with dsRNA (90 bp) |
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Components |
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-Supramolecule #1: Tetrameric TLR3 in complex with dsRNA (90 bp)
Supramolecule | Name: Tetrameric TLR3 in complex with dsRNA (90 bp) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#3 |
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Source (natural) | Organism: ![]() ![]() ![]() |
-Macromolecule #1: Toll-like receptor 3
Macromolecule | Name: Toll-like receptor 3 / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 77.365852 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: TNQCTVRYNV ADCSHLKLTH IPDDLPSNIT VLNLTHNQLR RLPPTNFTRY SQLAILDAGF NSISKLEPEL CQILPLLKVL NLQHNELSQ ISDQTFVFCT NLTELDLMSN SIHKIKSNPF KNQKNLIKLD LSHNGLSSTK LGTGVQLENL QELLLAKNKI L ALRSEELE ...String: TNQCTVRYNV ADCSHLKLTH IPDDLPSNIT VLNLTHNQLR RLPPTNFTRY SQLAILDAGF NSISKLEPEL CQILPLLKVL NLQHNELSQ ISDQTFVFCT NLTELDLMSN SIHKIKSNPF KNQKNLIKLD LSHNGLSSTK LGTGVQLENL QELLLAKNKI L ALRSEELE FLGNSSLRKL DLSSNPLKEF SPGCFQTIGK LFALLLNNAQ LNPHLTEKLC WELSNTSIQN LSLANNQLLA TS ESTFSGL KWTNLTQLDL SYNNLHDVGN GSFSYLPSLR YLSLEYNNIQ RLSPRSFYGL SNLRYLSLKR AFTKQSVSLA SHP NIDDFS FQWLKYLEYL NMDDNNIPST KSNTFTGLVS LKYLSLSKTF TSLQTLTNET FVSLAHSPLL TLNLTKNHIS KIAN GTFSW LGQLRILDLG LNEIEQKLSG QEWRGLRNIF EIYLSYNKYL QLSTSSFALV PSLQRLMLRR VALKNVDISP SPFRP LRNL TILDLSNNNI ANINEDLLEG LENLEILDFQ HNNLARLWKR ANPGGPVNFL KGLSHLHILN LESNGLDEIP VGVFKN LFE LKSINLGLNN LNKLEPFIFD DQTSLRSLNL QKNLITSVEK DVFGPPFQNL NSLDMRFNPF DCTCESISWF VNWINQT HT NISELSTHYL CNTPHHYYGF PLKLFDTSSC KDSAPFEL UniProtKB: ![]() |
-Macromolecule #2: RNA (81-MER)
Macromolecule | Name: RNA (81-MER) / type: rna / ID: 2 / Number of copies: 1 |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 25.699127 KDa |
Sequence | String: AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AUUUUUUUUU UUUUUUUUUU UUUUUUUUUU UUUUUUUUUU U |
-Macromolecule #3: RNA (81-MER)
Macromolecule | Name: RNA (81-MER) / type: rna / ID: 3 / Number of copies: 1 |
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Source (natural) | Organism: synthetic construct (others) |
Molecular weight | Theoretical: 25.676088 KDa |
Sequence | String: AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA AAAAAAAAAA UUUUUUUUUU UUUUUUUUUU UUUUUUUUUU UUUUUUUUUU U |
-Macromolecule #6: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 6 / Number of copies: 12 / Formula: NAG |
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Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ![]() ChemComp-NAG: |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Concentration | 0.2 mg/mL |
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Buffer | pH: 5.3 / Details: 25 mM MES-NaOH pH 5.3, 0.3 M NaCl |
Sugar embedding | Material: ice |
Vitrification | Cryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | JEOL CRYO ARM 300 |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
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Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 274002 |