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Yorodumi- PDB-3to4: Structure of mouse Valpha14Vbeta2-mouseCD1d-alpha-Galactosylceramide -
+Open data
-Basic information
Entry | Database: PDB / ID: 3to4 | |||||||||
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Title | Structure of mouse Valpha14Vbeta2-mouseCD1d-alpha-Galactosylceramide | |||||||||
Components |
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Keywords | IMMUNE SYSTEM / mouse CD1d / mouse NKT | |||||||||
Function / homology | Function and homology information regulation of immature T cell proliferation in thymus / positive regulation of NK T cell differentiation / lipid antigen binding / positive regulation of NK T cell activation / NK T cell differentiation / endogenous lipid antigen binding / exogenous lipid antigen binding / antigen processing and presentation, endogenous lipid antigen via MHC class Ib / antigen processing and presentation, exogenous lipid antigen via MHC class Ib / lipopeptide binding ...regulation of immature T cell proliferation in thymus / positive regulation of NK T cell differentiation / lipid antigen binding / positive regulation of NK T cell activation / NK T cell differentiation / endogenous lipid antigen binding / exogenous lipid antigen binding / antigen processing and presentation, endogenous lipid antigen via MHC class Ib / antigen processing and presentation, exogenous lipid antigen via MHC class Ib / lipopeptide binding / positive thymic T cell selection / positive regulation of macrophage activation / Endosomal/Vacuolar pathway / DAP12 interactions / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / DAP12 signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / regulation of membrane depolarization / antigen processing and presentation / positive regulation of interleukin-4 production / regulation of immune response / cellular defense response / positive regulation of T cell proliferation / positive regulation of interleukin-2 production / Neutrophil degranulation / cell adhesion molecule binding / T cell receptor binding / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / cellular response to iron(III) ion / negative regulation of forebrain neuron differentiation / peptide antigen assembly with MHC class I protein complex / response to molecule of bacterial origin / regulation of erythrocyte differentiation / regulation of iron ion transport / MHC class I peptide loading complex / HFE-transferrin receptor complex / T cell mediated cytotoxicity / cellular response to iron ion / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / MHC class I protein complex / multicellular organismal-level iron ion homeostasis / positive regulation of T cell mediated cytotoxicity / peptide antigen assembly with MHC class II protein complex / negative regulation of neurogenesis / MHC class II protein complex / positive regulation of receptor-mediated endocytosis / cellular response to nicotine / phagocytic vesicle membrane / peptide antigen binding / positive regulation of cellular senescence / antigen processing and presentation of exogenous peptide antigen via MHC class II / positive regulation of immune response / negative regulation of epithelial cell proliferation / positive regulation of T cell activation / antimicrobial humoral immune response mediated by antimicrobial peptide / positive regulation of type II interferon production / sensory perception of smell / negative regulation of neuron projection development / late endosome / MHC class II protein complex binding / late endosome membrane / T cell differentiation in thymus / antibacterial humoral response / iron ion transport / histone binding / protein refolding / protein homotetramerization / cellular response to lipopolysaccharide / intracellular iron ion homeostasis / defense response to Gram-negative bacterium / amyloid fibril formation / lysosome / learning or memory / early endosome / endosome membrane / defense response to Gram-positive bacterium / immune response / lysosomal membrane / external side of plasma membrane / innate immune response / structural molecule activity / Golgi apparatus / cell surface / endoplasmic reticulum / protein homodimerization activity / extracellular space / identical protein binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Mus musculus (house mouse) HOMO SAPIENS (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å | |||||||||
Authors | Patel, O. / Rossjohn, J. | |||||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2011 Title: Vbeta2 natural killer T cell antigen receptor-mediated recognition of CD1d-glycolipid antigen. Authors: Patel, O. / Pellicci, D.G. / Uldrich, A.P. / Sullivan, L.C. / Bhati, M. / McKnight, M. / Richardson, S.K. / Howell, A.R. / Mallevaey, T. / Zhang, J. / Bedel, R. / Besra, G.S. / Brooks, A.G. ...Authors: Patel, O. / Pellicci, D.G. / Uldrich, A.P. / Sullivan, L.C. / Bhati, M. / McKnight, M. / Richardson, S.K. / Howell, A.R. / Mallevaey, T. / Zhang, J. / Bedel, R. / Besra, G.S. / Brooks, A.G. / Kjer-Nielsen, L. / McCluskey, J. / Porcelli, S.A. / Gapin, L. / Rossjohn, J. / Godfrey, D.I. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3to4.cif.gz | 349.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3to4.ent.gz | 282.4 KB | Display | PDB format |
PDBx/mmJSON format | 3to4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/to/3to4 ftp://data.pdbj.org/pub/pdb/validation_reports/to/3to4 | HTTPS FTP |
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-Related structure data
Related structure data | 3he7S S: Starting model for refinement |
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Similar structure data |
-Links
-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: 34662.012 Da / Num. of mol.: 1 / Fragment: UNP residues 19-297 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Cd1d1, Cd1.1 / Plasmid: pBacp10pH / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P11609 |
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#2: Protein | Mass: 11660.350 Da / Num. of mol.: 1 / Fragment: UNP residues 21-119 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: B2m, RP23-34E24.5-001, mCG_11606 / Plasmid: pBacp10pH / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q91XJ8, UniProt: P01887*PLUS |
-Antibody , 2 types, 2 molecules CD
#3: Antibody | Mass: 23235.650 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: FOR CHAIN C, RESIDUES 1 TO 116 IS MOUSE VARIABLE DOMAIN AND 117-207 IS HUMAN CONSTANT DOMAIN Source: (gene. exp.) HOMO SAPIENS, Mus musculus / Plasmid: pET30b / Production host: Escherichia coli (E. coli) |
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#4: Antibody | Mass: 28895.248 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: FOR CHAIN D, RESIDUES 1 TO 117 IS MOUSE VARIABLE DOMAIN AND 118-247 IS HUMAN CONSTANT DOMAIN. Source: (gene. exp.) HOMO SAPIENS, Mus musculus / Plasmid: pET30b / Production host: Escherichia coli (E. coli) |
-Sugars , 3 types, 4 molecules
#5: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#6: Sugar | ChemComp-AGH / |
#7: Sugar |
-Non-polymers , 1 types, 5 molecules
#8: Water | ChemComp-HOH / |
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-Details
Sequence details | THE SWISS-PROT ENTRY P11609 CONFLICTS WITH BRADBURY ET AL., 1988 WHICH SUGGESTS A HISTIDINE IN ...THE SWISS-PROT ENTRY P11609 CONFLICTS WITH BRADBURY ET AL., 1988 WHICH SUGGESTS A HISTIDINE IN PLACE OF ASPARTATE. SEQUENCE IN THIS PDB AGREES WITH THE CITATION. RESIDUES AT THE END OF CHAIN C 'ENDGGGCK' ARE TAG REGION AND NOT PART OF THE ORIGINAL PROTEIN. RESIDUES AT THE END OF CHAIN D 'QDRGGGCD' ARE TAG REGION AND NOT PART OF THE ORIGINAL PROTEIN |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.96 Å3/Da / Density % sol: 58.47 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 17% PEG 10K, 0.1M ammonium acetate, 0.1M Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.95453 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 17, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.95453 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→82.64 Å / Num. obs: 22054 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9.7 % / Biso Wilson estimate: 64.6 Å2 / Rmerge(I) obs: 0.241 / Net I/σ(I): 10.3 |
Reflection shell | Resolution: 3.1→3.27 Å / Redundancy: 10.1 % / Rmerge(I) obs: 1.243 / Mean I/σ(I) obs: 2.8 / Num. unique all: 3160 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 3HE7 Resolution: 3.1→78.05 Å / Cor.coef. Fo:Fc: 0.912 / Cor.coef. Fo:Fc free: 0.875 / SU B: 47.693 / SU ML: 0.379 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R Free: 0.471 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 69.466 Å2
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Refinement step | Cycle: LAST / Resolution: 3.1→78.05 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.1→3.179 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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