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- PDB-1qrn: CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qrn | ||||||
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Title | CRYSTAL STRUCTURE OF HUMAN A6 TCR COMPLEXED WITH HLA-A2 BOUND TO ALTERED HTLV-1 TAX PEPTIDE P6A | ||||||
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Function / homology | ![]() alpha-beta T cell receptor complex / T cell mediated cytotoxicity directed against tumor cell target / positive regulation of memory T cell activation / TAP complex binding / Golgi medial cisterna / positive regulation of CD8-positive, alpha-beta T cell activation / CD8-positive, alpha-beta T cell activation / positive regulation of CD8-positive, alpha-beta T cell proliferation / CD8 receptor binding / Translocation of ZAP-70 to Immunological synapse ...alpha-beta T cell receptor complex / T cell mediated cytotoxicity directed against tumor cell target / positive regulation of memory T cell activation / TAP complex binding / Golgi medial cisterna / positive regulation of CD8-positive, alpha-beta T cell activation / CD8-positive, alpha-beta T cell activation / positive regulation of CD8-positive, alpha-beta T cell proliferation / CD8 receptor binding / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / antigen processing and presentation of exogenous peptide antigen via MHC class I / endoplasmic reticulum exit site / alpha-beta T cell activation / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent / Generation of second messenger molecules / TAP binding / PD-1 signaling / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Ding, Y.H. / Baker, B.M. / Garboczi, D.N. / Biddison, W.E. / Wiley, D.C. | ||||||
![]() | ![]() Title: Four A6-TCR/peptide/HLA-A2 structures that generate very different T cell signals are nearly identical. Authors: Ding, Y.H. / Baker, B.M. / Garboczi, D.N. / Biddison, W.E. / Wiley, D.C. #1: ![]() Title: Structure of the Complex between Human T-Cell Receptor, Viral Peptide and Hla-A2 Authors: Garboczi, D.N. / Ghosh, P. / Utz, U. / Fan, Q.R. / Wiley, D.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 172.1 KB | Display | ![]() |
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PDB format | ![]() | 140.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 31725.088 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Protein | ![]() Mass: 11879.356 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
-T-CELL RECEPTOR, ... , 2 types, 2 molecules DE
#4: Protein | ![]() Mass: 22130.264 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#5: Protein | ![]() Mass: 27175.199 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
-Protein/peptide / Non-polymers , 2 types, 52 molecules C![](data/chem/img/HOH.gif)
![](data/chem/img/HOH.gif)
#3: Protein/peptide | Mass: 1044.243 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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#6: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.81 Å3/Da / Density % sol: 56.26 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | Temperature: 287 K / Method: vapor diffusion, hanging drop / pH: 7 Details: seeding with hanging drop vapor diffusion; 50 mM MOPS pH 7.0, 75 mM MgSO4, 13% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 287K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.5 / Method: unknown | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Nov 26, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.8→25 Å / Num. all: 25985 / Num. obs: 25752 / Redundancy: 3.1 % / Rmerge(I) obs: 0.076 / Net I/σ(I): 15.1 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.26 |
Reflection | *PLUS Lowest resolution: 25 Å / % possible obs: 98.2 % |
Reflection shell | *PLUS % possible obs: 83.2 % / Mean I/σ(I) obs: 3.7 |
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Processing
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Refinement | Resolution: 2.8→25 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0
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Refinement step | Cycle: LAST / Resolution: 2.8→25 Å
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 25 Å / σ(F): 0 / % reflection Rfree: 10.5 % / Rfactor obs: 0.216 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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