+Open data
-Basic information
Entry | Database: PDB / ID: 7nt7 | ||||||
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Title | Solution structure of toll like receptor 1 (TLR1) TIR domain | ||||||
Components | Toll-like receptor 1 | ||||||
Keywords | SIGNALING PROTEIN / PROTEIN / TLR / toll like receptor / TIR domain / TLR1 | ||||||
Function / homology | Function and homology information Toll-like receptor 1-Toll-like receptor 2 protein complex / detection of triacyl bacterial lipopeptide / cellular response to triacyl bacterial lipopeptide / positive regulation of toll-like receptor 2 signaling pathway / Toll Like Receptor TLR1:TLR2 Cascade / Beta defensins / Toll-like receptor 2 binding / macrophage activation / Regulation of TLR by endogenous ligand / lipopeptide binding ...Toll-like receptor 1-Toll-like receptor 2 protein complex / detection of triacyl bacterial lipopeptide / cellular response to triacyl bacterial lipopeptide / positive regulation of toll-like receptor 2 signaling pathway / Toll Like Receptor TLR1:TLR2 Cascade / Beta defensins / Toll-like receptor 2 binding / macrophage activation / Regulation of TLR by endogenous ligand / lipopeptide binding / NAD+ nucleotidase, cyclic ADP-ribose generating / NADP+ nucleosidase activity / MyD88 deficiency (TLR2/4) / IRAK4 deficiency (TLR2/4) / MyD88:MAL(TIRAP) cascade initiated on plasma membrane / toll-like receptor signaling pathway / positive regulation of interleukin-8 production / positive regulation of interleukin-6 production / phagocytic vesicle membrane / transmembrane signaling receptor activity / positive regulation of tumor necrosis factor production / signaling receptor activity / ER-Phagosome pathway / receptor complex / immune response / inflammatory response / membrane raft / innate immune response / SARS-CoV-2 activates/modulates innate and adaptive immune responses / Golgi apparatus / signal transduction / membrane / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Mineev, K.S. / Lushpa, V.A. / Goncharuk, M.V. | ||||||
Funding support | Russian Federation, 1items
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Citation | Journal: Commun Biol / Year: 2021 Title: Modulation of Toll-like receptor 1 intracellular domain structure and activity by Zn 2+ ions. Authors: Lushpa, V.A. / Goncharuk, M.V. / Lin, C. / Zalevsky, A.O. / Talyzina, I.A. / Luginina, A.P. / Vakhrameev, D.D. / Shevtsov, M.B. / Goncharuk, S.A. / Arseniev, A.S. / Borshchevskiy, V.I. / Wang, X. / Mineev, K.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7nt7.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb7nt7.ent.gz | 918.5 KB | Display | PDB format |
PDBx/mmJSON format | 7nt7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nt/7nt7 ftp://data.pdbj.org/pub/pdb/validation_reports/nt/7nt7 | HTTPS FTP |
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-Related structure data
Related structure data | 7nuwC 7nuxC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 19204.139 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TLR1, KIAA0012 / Production host: Escherichia coli (E. coli) References: UniProt: Q15399, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Type: solution Contents: 0.8 mM [U-100% 13C; U-100% 15N] TLR1-TIR, 20 mM PIPES, 25 mM sodium chloride, 3 mM TCEP, 95% H2O/5% D2O Label: s1 / Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 50 mM / Label: sc1 / pH: 6.3 / Pressure: AMBIENT Pa / Temperature: 308 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III / Manufacturer: Bruker / Model: AVANCE III / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 200 / Conformers submitted total number: 20 |