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Yorodumi- PDB-3eo1: Structure of the Fab Fragment of GC-1008 in Complex with Transfor... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3eo1 | ||||||
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Title | Structure of the Fab Fragment of GC-1008 in Complex with Transforming Growth Factor-Beta 3 | ||||||
Components |
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Keywords | IMMUNE SYSTEM/CYTOKINE / Antibody-cytokine complex / Growth factor / FAB fragment / Cardiomyopathy / Cleavage on pair of basic residues / Glycoprotein / Mitogen / Polymorphism / Secreted / IMMUNE SYSTEM-CYTOKINE COMPLEX | ||||||
Function / homology | Function and homology information uterine wall breakdown / detection of hypoxia / frontal suture morphogenesis / embryonic neurocranium morphogenesis / type III transforming growth factor beta receptor binding / positive regulation of tight junction disassembly / negative regulation of macrophage cytokine production / secondary palate development / response to laminar fluid shear stress / type II transforming growth factor beta receptor binding ...uterine wall breakdown / detection of hypoxia / frontal suture morphogenesis / embryonic neurocranium morphogenesis / type III transforming growth factor beta receptor binding / positive regulation of tight junction disassembly / negative regulation of macrophage cytokine production / secondary palate development / response to laminar fluid shear stress / type II transforming growth factor beta receptor binding / type I transforming growth factor beta receptor binding / mammary gland development / cell-cell junction organization / transforming growth factor beta binding / digestive tract development / IgG immunoglobulin complex / face morphogenesis / odontogenesis / Molecules associated with elastic fibres / positive regulation of filopodium assembly / Classical antibody-mediated complement activation / Initial triggering of complement / lung alveolus development / TGF-beta receptor signaling activates SMADs / negative regulation of vascular associated smooth muscle cell proliferation / positive regulation of SMAD protein signal transduction / inner ear development / positive regulation of cell division / FCGR activation / ECM proteoglycans / positive regulation of collagen biosynthetic process / Role of phospholipids in phagocytosis / positive regulation of epithelial to mesenchymal transition / salivary gland morphogenesis / immunoglobulin complex, circulating / positive regulation of stress fiber assembly / immunoglobulin receptor binding / T-tubule / FCGR3A-mediated IL10 synthesis / transforming growth factor beta receptor signaling pathway / platelet alpha granule lumen / complement activation, classical pathway / cytokine activity / Regulation of Complement cascade / response to progesterone / female pregnancy / positive regulation of protein secretion / antigen binding / FCGR3A-mediated phagocytosis / B cell receptor signaling pathway / negative regulation of transforming growth factor beta receptor signaling pathway / growth factor activity / Regulation of actin dynamics for phagocytic cup formation / response to estrogen / Platelet degranulation / regulation of cell population proliferation / antibacterial humoral response / Interleukin-4 and Interleukin-13 signaling / collagen-containing extracellular matrix / adaptive immune response / in utero embryonic development / negative regulation of neuron apoptotic process / positive regulation of MAPK cascade / blood microparticle / response to hypoxia / positive regulation of apoptotic process / negative regulation of cell population proliferation / intracellular membrane-bounded organelle / neuronal cell body / positive regulation of cell population proliferation / protein-containing complex binding / positive regulation of DNA-templated transcription / cell surface / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular exosome / extracellular region / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å | ||||||
Authors | Gruetter, C. / Gruetter, M.G. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2008 Title: A cytokine-neutralizing antibody as a structural mimetic of 2 receptor interactions Authors: Wilkinson, T. / Turner, R. / Podichetty, S. / Finch, D. / McCourt, M. / Loning, S. / Jermutus, L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3eo1.cif.gz | 376.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3eo1.ent.gz | 315.8 KB | Display | PDB format |
PDBx/mmJSON format | 3eo1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3eo1_validation.pdf.gz | 524.1 KB | Display | wwPDB validaton report |
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Full document | 3eo1_full_validation.pdf.gz | 618.1 KB | Display | |
Data in XML | 3eo1_validation.xml.gz | 83.2 KB | Display | |
Data in CIF | 3eo1_validation.cif.gz | 111.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eo/3eo1 ftp://data.pdbj.org/pub/pdb/validation_reports/eo/3eo1 | HTTPS FTP |
-Related structure data
Related structure data | 3eo0SC 1tgjS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Antibody | Mass: 23425.934 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse) / Strain (production host): NS0 #2: Antibody | Mass: 23838.779 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse) / Strain (production host): NS0 / References: UniProt: P01861*PLUS #3: Protein | Mass: 12734.504 Da / Num. of mol.: 4 / Fragment: UNP residues 301-412, receptor binding fragment Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TGFB3 / Production host: Escherichia coli (E. coli) / References: UniProt: P10600 Sequence details | A SEQUENCE DATABASE REFERENCE FOR THIS PROTEIN (ANTIBODY) DOES NOT CURRENTLY EXIST. | |
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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: 3.47 Å3/Da / Density % sol: 64.5 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.8 Details: 23% tert.-butanol, 0.1M sodium citrate, 0.2M phenoxyacetic acid, pH6.8, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.070645 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 24, 2006 / Details: BENT MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.070645 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→35 Å / Num. obs: 60296 / % possible obs: 97.9 % / Redundancy: 5 % / Rmerge(I) obs: 0.092 / Rsym value: 0.077 / Net I/σ(I): 20.8 |
Reflection shell | Resolution: 3.1→3.3 Å / Redundancy: 5 % / Rmerge(I) obs: 0.367 / Mean I/σ(I) obs: 3.8 / Num. unique all: 10322 / Rsym value: 0.522 / % possible all: 96.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3EO0, 1TGJ Resolution: 3.1→35 Å / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Displacement parameters | Biso mean: 80.7 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→35 Å
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Refine LS restraints |
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