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Yorodumi- PDB-5ylx: Integrated illustration of a valid epitope based on the SLA class... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5ylx | ||||||||||||
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Title | Integrated illustration of a valid epitope based on the SLA class I structure and tetramer technique could carry forward the development of molecular vaccine in swine species | ||||||||||||
Components |
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Keywords | IMMUNE SYSTEM / MHC / CTL response / tetramer | ||||||||||||
Function / homology | Function and homology information ER-Phagosome pathway / Endosomal/Vacuolar pathway / DAP12 interactions / DAP12 signaling / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / symbiont-mediated suppression of host PKR/eIFalpha signaling / Neutrophil degranulation / protein serine/threonine kinase inhibitor activity / antigen processing and presentation of peptide antigen via MHC class I ...ER-Phagosome pathway / Endosomal/Vacuolar pathway / DAP12 interactions / DAP12 signaling / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / symbiont-mediated suppression of host PKR/eIFalpha signaling / Neutrophil degranulation / protein serine/threonine kinase inhibitor activity / antigen processing and presentation of peptide antigen via MHC class I / host cell endoplasmic reticulum / Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / host cell membrane / RNA nuclease activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / antigen processing and presentation of endogenous peptide antigen via MHC class Ib / antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent / lumenal side of endoplasmic reticulum membrane / MHC class I protein complex / peptide antigen assembly with MHC class II protein complex / MHC class II protein complex / positive regulation of T cell mediated cytotoxicity / phagocytic vesicle membrane / peptide antigen binding / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / positive regulation of T cell activation / MHC class II protein complex binding / Lyases; Phosphorus-oxygen lyases / late endosome membrane / symbiont-mediated suppression of host NF-kappaB cascade / symbiont-mediated suppression of host ISG15-protein conjugation / symbiont-mediated perturbation of host ubiquitin-like protein modification / endonuclease activity / DNA helicase / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / RNA helicase activity / host cell perinuclear region of cytoplasm / viral protein processing / lyase activity / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / immune response / RNA-directed RNA polymerase / viral translational frameshifting / external side of plasma membrane / lysosomal membrane / viral RNA genome replication / cysteine-type endopeptidase activity / serine-type endopeptidase activity / RNA-dependent RNA polymerase activity / signaling receptor binding / virus-mediated perturbation of host defense response / nucleotide binding / DNA-templated transcription / host cell nucleus / ATP hydrolysis activity / proteolysis / RNA binding / extracellular space / zinc ion binding / extracellular region / ATP binding / membrane Similarity search - Function | ||||||||||||
Biological species | Sus scrofa (pig) Porcine reproductive and respiratory syndrome virus | ||||||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.2 Å | ||||||||||||
Authors | Pan, X.C. / Wei, X.H. / Zhang, N. / Xia, C. | ||||||||||||
Funding support | China, 3items
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Citation | Journal: Front Immunol / Year: 2019 Title: Illumination of PRRSV Cytotoxic T Lymphocyte Epitopes by the Three-Dimensional Structure and Peptidome of Swine Lymphocyte Antigen Class I (SLA-I). Authors: Pan, X. / Zhang, N. / Wei, X. / Jiang, Y. / Chen, R. / Li, Q. / Liang, R. / Zhang, L. / Ma, L. / Xia, C. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ylx.cif.gz | 177.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ylx.ent.gz | 140.2 KB | Display | PDB format |
PDBx/mmJSON format | 5ylx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5ylx_validation.pdf.gz | 439.5 KB | Display | wwPDB validaton report |
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Full document | 5ylx_full_validation.pdf.gz | 443.7 KB | Display | |
Data in XML | 5ylx_validation.xml.gz | 20 KB | Display | |
Data in CIF | 5ylx_validation.cif.gz | 29.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/yl/5ylx ftp://data.pdbj.org/pub/pdb/validation_reports/yl/5ylx | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 31399.844 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Gene: SLA-1 / Production host: Escherichia coli (E. coli) / References: UniProt: H6TIB1 |
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#2: Protein | Mass: 11431.918 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / Gene: B2M / Production host: Escherichia coli (E. coli) / References: UniProt: Q07717 |
#3: Protein/peptide | Mass: 1054.215 Da / Num. of mol.: 1 / Source method: obtained synthetically Source: (synth.) Porcine reproductive and respiratory syndrome virus References: UniProt: I6YDJ5, UniProt: Q9YN02*PLUS |
#4: Water | ChemComp-HOH / |
Has protein modification | Y |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.24 % |
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Crystal grow | Temperature: 277.15 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: 0.1M Ammonium acetate, 0.1M BIS-TRIS pH5.5, 17% PEG 10000, temperature 277.15K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54178 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Aug 5, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→50 Å / Num. obs: 24678 / % possible obs: 99.5 % / Redundancy: 7.9 % / Rmerge(I) obs: 0.083 / Rsym value: 0.083 / Net I/σ(I): 27.366 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 7.9 % / Rmerge(I) obs: 0.286 / Mean I/σ(I) obs: 7.517 / Rsym value: 0.286 / % possible all: 98.9 |
-Processing
Software |
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Refinement | Resolution: 2.2→29.607 Å / SU ML: 0.3 / Cross valid method: NONE / σ(F): 0.14 / Phase error: 21.63
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Bsol: 40.016 Å2 / ksol: 0.4 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.2→29.607 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: -7.1259 Å / Origin y: 25.8216 Å / Origin z: 15.7159 Å
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Refinement TLS group | Selection details: all |