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Yorodumi- PDB-1zsd: Crystal Structure Of HLA-B*3501 Presenting an 11-Mer EBV Antigen ... -
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Basic information
| Entry | Database: PDB / ID: 1zsd | ||||||
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| Title | Crystal Structure Of HLA-B*3501 Presenting an 11-Mer EBV Antigen EPLPQGQLTAY | ||||||
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Keywords | IMMUNE SYSTEM / Human leukocyte antigen / major histocompatibility complex I / B35 / B*3501 / bulged peptide | ||||||
| Function / homology | Function and homology informationsymbiont-mediated suppression of host tumor necrosis factor-mediated signaling pathway / symbiont-mediated perturbation of host cell cycle G0/G1 transition checkpoint / release from viral latency / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity / regulation of interleukin-12 production / regulation of dendritic cell differentiation / regulation of T cell anergy / regulation of interleukin-6 production / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / TAP binding ...symbiont-mediated suppression of host tumor necrosis factor-mediated signaling pathway / symbiont-mediated perturbation of host cell cycle G0/G1 transition checkpoint / release from viral latency / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity / regulation of interleukin-12 production / regulation of dendritic cell differentiation / regulation of T cell anergy / regulation of interleukin-6 production / symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint / TAP binding / protection from natural killer cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / detection of bacterium / secretory granule membrane / negative regulation of receptor binding / early endosome lumen / Nef mediated downregulation of MHC class I complex cell surface expression / DAP12 interactions / transferrin transport / cellular response to iron ion / lumenal side of endoplasmic reticulum membrane / Endosomal/Vacuolar pathway / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / peptide antigen assembly with MHC class II protein complex / cellular response to iron(III) ion / MHC class II protein complex / negative regulation of forebrain neuron differentiation / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / ER to Golgi transport vesicle membrane / peptide antigen assembly with MHC class I protein complex / regulation of iron ion transport / regulation of erythrocyte differentiation / HFE-transferrin receptor complex / response to molecule of bacterial origin / MHC class I peptide loading complex / defense response / T cell mediated cytotoxicity / positive regulation of T cell cytokine production / antigen processing and presentation of endogenous peptide antigen via MHC class I / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / MHC class I protein complex / positive regulation of T cell activation / peptide antigen binding / positive regulation of receptor-mediated endocytosis / negative regulation of neurogenesis / cellular response to nicotine / positive regulation of T cell mediated cytotoxicity / multicellular organismal-level iron ion homeostasis / specific granule lumen / phagocytic vesicle membrane / recycling endosome membrane / Interferon gamma signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / negative regulation of epithelial cell proliferation / MHC class II protein complex binding / Interferon alpha/beta signaling / Modulation by Mtb of host immune system / late endosome membrane / sensory perception of smell / positive regulation of cellular senescence / tertiary granule lumen / DAP12 signaling / T cell differentiation in thymus / protein-folding chaperone binding / negative regulation of neuron projection development / ER-Phagosome pathway / protein refolding / early endosome membrane / protein homotetramerization / adaptive immune response / sequence-specific DNA binding / amyloid fibril formation / intracellular iron ion homeostasis / learning or memory / protein dimerization activity / immune response / endoplasmic reticulum lumen / DNA-binding transcription factor activity / Amyloid fiber formation / Golgi membrane / signaling receptor binding / lysosomal membrane / innate immune response / external side of plasma membrane / focal adhesion / Neutrophil degranulation / regulation of DNA-templated transcription / chromatin / positive regulation of DNA-templated transcription / host cell nucleus / SARS-CoV-2 activates/modulates innate and adaptive immune responses / structural molecule activity / cell surface / endoplasmic reticulum / Golgi apparatus / protein homodimerization activity / extracellular space / DNA binding Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Miles, J.J. / Elhassen, D. / Borg, N.A. / Silins, S.L. / Tynan, F.E. / Burrows, J.M. / Purcell, A.W. / Kjer-Nielsen, L. / Rossjohn, J. / Burrows, S.R. / McCluskey, J. | ||||||
Citation | Journal: J.Immunol. / Year: 2005Title: CTL Recognition of a Bulged Viral Peptide Involves Biased TCR Selection. Authors: Miles, J.J. / Elhassen, D. / Borg, N.A. / Silins, S.L. / Tynan, F.E. / Burrows, J.M. / Purcell, A.W. / Kjer-Nielsen, L. / Rossjohn, J. / Burrows, S.R. / McCluskey, J. / El-Hassen, D. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1zsd.cif.gz | 100.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1zsd.ent.gz | 75.6 KB | Display | PDB format |
| PDBx/mmJSON format | 1zsd.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1zsd_validation.pdf.gz | 443.5 KB | Display | wwPDB validaton report |
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| Full document | 1zsd_full_validation.pdf.gz | 449 KB | Display | |
| Data in XML | 1zsd_validation.xml.gz | 20.4 KB | Display | |
| Data in CIF | 1zsd_validation.cif.gz | 30.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zs/1zsd ftp://data.pdbj.org/pub/pdb/validation_reports/zs/1zsd | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1a1nS S: Starting model for refinement |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 31940.246 Da / Num. of mol.: 1 / Fragment: extracellular domains alpha-1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HLA-B, HLAB / Plasmid: pET30 / Production host: ![]() |
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| #2: Protein | Mass: 11748.160 Da / Num. of mol.: 1 / Fragment: beta-2-microglobulin Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: B2M / Plasmid: pET30 / Production host: ![]() |
| #3: Protein/peptide | Mass: 1216.339 Da / Num. of mol.: 1 / Fragment: EBV peptide EPLPQGQLTAY / Source method: obtained synthetically / References: UniProt: P03206 |
| #4: Water | ChemComp-HOH / |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 51.1 % |
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| Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.6 Details: 0.2M ammonium acetate, 17% w/v PEG 3350, 100mM cacodylate, pH 7.6, VAPOR DIFFUSION, HANGING DROP |
-Data collection
| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 14-BM-C / Wavelength: 1.5418 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 25, 2003 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 1.7→100 Å / Num. obs: 47652 / % possible obs: 93.4 % / Rmerge(I) obs: 0.079 / Χ2: 1.242 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 1A1N Resolution: 1.7→25.5 Å / σ(F): 0
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| Solvent computation | Bsol: 46.32 Å2 | ||||||||||||||||||||||||
| Displacement parameters | Biso mean: 21.858 Å2
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| Refinement step | Cycle: LAST / Resolution: 1.7→25.5 Å
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| Xplor file |
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Homo sapiens (human)
X-RAY DIFFRACTION
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