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Yorodumi- PDB-6bfs: The mechanism of GM-CSF inhibition by human GM-CSF auto-antibodies -
+Open data
-Basic information
Entry | Database: PDB / ID: 6bfs | ||||||
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Title | The mechanism of GM-CSF inhibition by human GM-CSF auto-antibodies | ||||||
Components |
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Keywords | IMMUNE SYSTEM / Cytokine-Fab complex / Pulmonary Alveolar Proteinosis / receptor assembly / autoantibodies | ||||||
Function / homology | Function and homology information granulocyte macrophage colony-stimulating factor receptor binding / neutrophil differentiation / histamine secretion / response to silicon dioxide / epithelial fluid transport / positive regulation of interleukin-23 production / regulation of circadian sleep/wake cycle, sleep / dendritic cell differentiation / positive regulation of macrophage derived foam cell differentiation / response to fluid shear stress ...granulocyte macrophage colony-stimulating factor receptor binding / neutrophil differentiation / histamine secretion / response to silicon dioxide / epithelial fluid transport / positive regulation of interleukin-23 production / regulation of circadian sleep/wake cycle, sleep / dendritic cell differentiation / positive regulation of macrophage derived foam cell differentiation / response to fluid shear stress / myeloid dendritic cell differentiation / granulocyte macrophage colony-stimulating factor receptor complex / granulocyte-macrophage colony-stimulating factor signaling pathway / positive regulation of leukocyte proliferation / myeloid cell differentiation / cellular response to granulocyte macrophage colony-stimulating factor stimulus / RUNX1 regulates transcription of genes involved in differentiation of myeloid cells / positive regulation of podosome assembly / Interleukin-10 signaling / monocyte differentiation / cell surface receptor signaling pathway via JAK-STAT / macrophage differentiation / Interleukin-3, Interleukin-5 and GM-CSF signaling / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / embryonic placenta development / Interleukin receptor SHC signaling / positive regulation of tyrosine phosphorylation of STAT protein / cytokine activity / growth factor activity / RAF/MAP kinase cascade / cellular response to lipopolysaccharide / cell population proliferation / positive regulation of cell migration / immune response / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / positive regulation of gene expression / extracellular space / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2 Å | ||||||
Authors | Dhagat, U. / Hercus, T.R. / Broughton, S.E. / Nero, T.L. / Lopez, A.F. / Parker, M.W. | ||||||
Funding support | Australia, 1items
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Citation | Journal: MAbs / Year: 2018 Title: The mechanism of GM-CSF inhibition by human GM-CSF auto-antibodies suggests novel therapeutic opportunities. Authors: Dhagat, U. / Hercus, T.R. / Broughton, S.E. / Nero, T.L. / Cheung Tung Shing, K.S. / Barry, E.F. / Thomson, C.A. / Bryson, S. / Pai, E.F. / McClure, B.J. / Schrader, J.W. / Lopez, A.F. / Parker, M.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6bfs.cif.gz | 119.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6bfs.ent.gz | 89.9 KB | Display | PDB format |
PDBx/mmJSON format | 6bfs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6bfs_validation.pdf.gz | 432.3 KB | Display | wwPDB validaton report |
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Full document | 6bfs_full_validation.pdf.gz | 433.9 KB | Display | |
Data in XML | 6bfs_validation.xml.gz | 20.3 KB | Display | |
Data in CIF | 6bfs_validation.cif.gz | 29 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bf/6bfs ftp://data.pdbj.org/pub/pdb/validation_reports/bf/6bfs | HTTPS FTP |
-Related structure data
Related structure data | 6bfqC 1rjlS C: citing same article (ref.) 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
#1: Antibody | Mass: 23449.902 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) |
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#2: Antibody | Mass: 23270.219 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) |
#3: Protein | Mass: 14492.495 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CSF2, GMCSF / Production host: Escherichia coli (E. coli) / References: UniProt: P04141 |
#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: 2.12 Å3/Da / Density % sol: 41.92 % |
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Crystal grow | Temperature: 283.15 K / Method: vapor diffusion, hanging drop Details: 0. 2 M Sodium Chloride, 20% PEG 8000, 0.1 M phosphate Citrate 4.5 |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.954 Å | ||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 3, 2015 | ||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.954 Å / Relative weight: 1 | ||||||||||||||||||||||||
Reflection | Resolution: 2→40 Å / Num. obs: 34696 / % possible obs: 99.4 % / Redundancy: 3.7 % / CC1/2: 0.998 / Rmerge(I) obs: 0.074 / Rpim(I) all: 0.045 / Rrim(I) all: 0.087 / Net I/σ(I): 12 | ||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1
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-Phasing
Phasing | Method: molecular replacement | |||||||||
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Phasing MR | Model details: Phaser MODE: MR_AUTO
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1RJL Resolution: 2→40 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.927 / SU B: 5.216 / SU ML: 0.141 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.191 / ESU R Free: 0.181 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 104.21 Å2 / Biso mean: 34.652 Å2 / Biso min: 16.13 Å2
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Refinement step | Cycle: final / Resolution: 2→40 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.001→2.053 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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