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Yorodumi- PDB-6gff: Structure of GARP (LRRC32) in complex with latent TGF-beta1 and M... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6gff | |||||||||
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Title | Structure of GARP (LRRC32) in complex with latent TGF-beta1 and MHG-8 Fab | |||||||||
Components |
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Keywords | IMMUNE SYSTEM / GARP / TGF-B1 / Activation / Treg | |||||||||
Function / homology | Function and homology information : / positive regulation of primary miRNA processing / positive regulation of microglia differentiation / Influenza Virus Induced Apoptosis / negative regulation of skeletal muscle tissue development / TGFBR2 MSI Frameshift Mutants in Cancer / regulatory T cell differentiation / regulation of blood vessel remodeling / regulation of striated muscle tissue development / extracellular matrix assembly ...: / positive regulation of primary miRNA processing / positive regulation of microglia differentiation / Influenza Virus Induced Apoptosis / negative regulation of skeletal muscle tissue development / TGFBR2 MSI Frameshift Mutants in Cancer / regulatory T cell differentiation / regulation of blood vessel remodeling / regulation of striated muscle tissue development / extracellular matrix assembly / negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / regulation of protein import into nucleus / embryonic liver development / type III transforming growth factor beta receptor binding / negative regulation of hyaluronan biosynthetic process / positive regulation of cardiac muscle cell differentiation / myofibroblast differentiation / odontoblast differentiation / connective tissue replacement involved in inflammatory response wound healing / positive regulation of receptor signaling pathway via STAT / negative regulation of macrophage cytokine production / TGFBR2 Kinase Domain Mutants in Cancer / : / positive regulation of isotype switching to IgA isotypes / positive regulation of mesenchymal stem cell proliferation / secondary palate development / membrane protein intracellular domain proteolysis / SMAD2/3 Phosphorylation Motif Mutants in Cancer / TGFBR1 KD Mutants in Cancer / heart valve morphogenesis / positive regulation of vasculature development / hyaluronan catabolic process / regulation of transforming growth factor beta receptor signaling pathway / ATP biosynthetic process / receptor catabolic process / positive regulation of extracellular matrix assembly / negative regulation of extracellular matrix disassembly / type II transforming growth factor beta receptor binding / TGFBR1 LBD Mutants in Cancer / positive regulation of chemotaxis / type I transforming growth factor beta receptor binding / negative regulation of biomineral tissue development / cell-cell junction organization / negative regulation of myoblast differentiation / positive regulation of vascular permeability / deubiquitinase activator activity / transforming growth factor beta binding / positive regulation of endothelial cell apoptotic process / response to cholesterol / positive regulation of chemokine (C-X-C motif) ligand 2 production / aortic valve morphogenesis / positive regulation of fibroblast migration / phosphate-containing compound metabolic process / negative regulation of protein localization to plasma membrane / sprouting angiogenesis / neural tube development / Molecules associated with elastic fibres / RUNX3 regulates CDKN1A transcription / negative regulation of cytokine production / positive regulation of epidermal growth factor receptor signaling pathway / ventricular cardiac muscle tissue morphogenesis / negative regulation of fat cell differentiation / macrophage derived foam cell differentiation / Syndecan interactions / negative regulation of cell-cell adhesion / positive regulation of interleukin-17 production / negative regulation of blood vessel endothelial cell migration / TGF-beta receptor signaling activates SMADs / negative regulation of activated T cell proliferation / plasma membrane => GO:0005886 / negative regulation of cell differentiation / positive regulation of SMAD protein signal transduction / RUNX3 regulates p14-ARF / positive regulation of cell division / cellular response to low-density lipoprotein particle stimulus / negative regulation of cell cycle / ECM proteoglycans / positive regulation of vascular endothelial growth factor production / epithelial to mesenchymal transition / positive regulation of collagen biosynthetic process / positive regulation of epithelial to mesenchymal transition / positive regulation of blood vessel endothelial cell migration / lymph node development / vasculogenesis / chondrocyte differentiation / hematopoietic progenitor cell differentiation / salivary gland morphogenesis / regulation of cell migration / extrinsic apoptotic signaling pathway / positive regulation of protein dephosphorylation / cellular response to transforming growth factor beta stimulus / antigen binding / extracellular matrix / positive regulation of protein metabolic process / protein export from nucleus / Downregulation of TGF-beta receptor signaling / transforming growth factor beta receptor signaling pathway / positive regulation of superoxide anion generation / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / negative regulation of miRNA transcription Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) Mus musculus (house mouse) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å | |||||||||
Authors | Merceron, R. / Lienart, S. / Vanderaa, C. / Colau, D. / Stockis, J. / Van Der Woning, B. / De Haard, H. / Saunders, M. / Coulie, P.G. / Savvides, S.N. / Lucas, S. | |||||||||
Funding support | Belgium, 2items
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Citation | Journal: Science / Year: 2018 Title: Structural basis of latent TGF-beta 1 presentation and activation by GARP on human regulatory T cells. Authors: Lienart, S. / Merceron, R. / Vanderaa, C. / Lambert, F. / Colau, D. / Stockis, J. / van der Woning, B. / De Haard, H. / Saunders, M. / Coulie, P.G. / Savvides, S.N. / Lucas, S. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6gff.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb6gff.ent.gz | 928.1 KB | Display | PDB format |
PDBx/mmJSON format | 6gff.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gf/6gff ftp://data.pdbj.org/pub/pdb/validation_reports/gf/6gff | HTTPS FTP |
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-Related structure data
Similar structure data |
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-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
-Transforming growth factor beta- ... , 2 types, 8 molecules ACEGBDFH
#1: Protein | Mass: 28531.488 Da / Num. of mol.: 4 / Fragment: LAP Source method: isolated from a genetically manipulated source Details: Mature protein expected to start at Leucine30. Obtained after cleavage of Pro-TGF-b1 by Furin after Arginine278. Source: (gene. exp.) Homo sapiens (human) / Gene: TGFB1, TGFB / Production host: Homo sapiens (human) / References: UniProt: P01137 #2: Protein | Mass: 12809.812 Da / Num. of mol.: 4 / Fragment: Mature Source method: isolated from a genetically manipulated source Details: Obtained after cleavage of Pro-TGF-b1 by Furin after Arginine278. Source: (gene. exp.) Homo sapiens (human) / Gene: TGFB1, TGFB / Production host: Homo sapiens (human) / References: UniProt: P01137 |
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-Protein , 1 types, 2 molecules IJ
#3: Protein | Mass: 67235.578 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: Mature protein expected to start at Histidine20. / Source: (gene. exp.) Homo sapiens (human) / Gene: LRRC32, D11S833E, GARP / Production host: Homo sapiens (human) / References: UniProt: Q14392 |
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-Antibody , 2 types, 4 molecules KMLN
#4: Antibody | Mass: 23376.770 Da / Num. of mol.: 2 / Source method: isolated from a natural source Details: Mature protein expected to start at Aspartic acid21. Source: (natural) Mus musculus (house mouse) #5: Antibody | Mass: 23832.617 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Mature protein expected to start at Glutamine20. / Source: (natural) Mus musculus (house mouse) |
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-Sugars , 3 types, 7 molecules
#6: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #7: 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 #8: Polysaccharide | alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-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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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.3 Å3/Da / Density % sol: 62.67 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / Details: 15% (w/v) PEG4000, 0.1 M HEPES pH 6.75 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.00001 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 27, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.00001 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→50 Å / Num. obs: 84967 / % possible obs: 90.1 % / Redundancy: 2.3 % / Biso Wilson estimate: 77.7 Å2 / Net I/σ(I): 8.15 |
Reflection shell | Resolution: 3.1→3.18 Å / Redundancy: 2.2 % / Num. unique obs: 6320 / % possible all: 90.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.1→29.921 Å / SU ML: 0.48 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 29.07
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→29.921 Å
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Refine LS restraints |
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LS refinement shell |
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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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