+Open data
-Basic information
Entry | Database: PDB / ID: 5gn0 | ||||||
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Title | Structure of TAZ-TEAD complex | ||||||
Components |
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Keywords | TRANSCRIPTION | ||||||
Function / homology | Function and homology information regulation of SMAD protein signal transduction / RUNX3 regulates YAP1-mediated transcription / YAP1- and WWTR1 (TAZ)-stimulated gene expression / kidney morphogenesis / Signaling by Hippo / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / trophectodermal cell fate commitment / regulation of metanephric nephron tubule epithelial cell differentiation / mesenchymal cell differentiation / heart process ...regulation of SMAD protein signal transduction / RUNX3 regulates YAP1-mediated transcription / YAP1- and WWTR1 (TAZ)-stimulated gene expression / kidney morphogenesis / Signaling by Hippo / SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription / trophectodermal cell fate commitment / regulation of metanephric nephron tubule epithelial cell differentiation / mesenchymal cell differentiation / heart process / stem cell division / hippo signaling / tissue homeostasis / glomerulus development / blastocyst formation / regulation of canonical Wnt signaling pathway / cell fate specification / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / positive regulation of stem cell population maintenance / negative regulation of fat cell differentiation / cilium assembly / cell fate commitment / embryonic organ development / positive regulation of osteoblast differentiation / positive regulation of epithelial to mesenchymal transition / embryo implantation / negative regulation of protein phosphorylation / protein-DNA complex / negative regulation of protein kinase activity / negative regulation of canonical Wnt signaling pathway / multicellular organism growth / positive regulation of protein localization to nucleus / osteoblast differentiation / transcription corepressor activity / DNA-binding transcription activator activity, RNA polymerase II-specific / in utero embryonic development / transcription regulator complex / sequence-specific DNA binding / transcription coactivator activity / nuclear body / DNA-binding transcription factor activity, RNA polymerase II-specific / protein ubiquitination / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / DNA-templated transcription / positive regulation of cell population proliferation / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å | ||||||
Authors | Kaan, H.Y.K. / Song, H. | ||||||
Citation | Journal: Sci Rep / Year: 2017 Title: Crystal structure of TAZ-TEAD complex reveals a distinct interaction mode from that of YAP-TEAD complex Authors: Kaan, H.Y.K. / Chan, S.W. / Tan, S.K.J. / Guo, F. / Lim, C.J. / Hong, W. / Song, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5gn0.cif.gz | 214.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5gn0.ent.gz | 172.4 KB | Display | PDB format |
PDBx/mmJSON format | 5gn0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gn/5gn0 ftp://data.pdbj.org/pub/pdb/validation_reports/gn/5gn0 | HTTPS FTP |
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-Related structure data
Related structure data | 3juaS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 26416.885 Da / Num. of mol.: 4 / Fragment: UNP residues 210-427 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: TEAD4 / Production host: Escherichia coli (E. coli) / References: UniProt: Q62296 #2: Protein/peptide | Mass: 4082.652 Da / Num. of mol.: 4 / Fragment: UNP residues 24-57 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Taz / Production host: Escherichia coli (E. coli) / References: UniProt: Q9EPK5 #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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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: 3.88 Å3/Da / Density % sol: 68.3 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.2 Details: 6% Polyethylene glycol 10000, 0.05M magnesium acetate, 0.1M tri-sodium citrate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSRRC / Beamline: BL13C1 / Wavelength: 0.975 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: May 2, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.975 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→30 Å / Num. obs: 42312 / % possible obs: 98.6 % / Redundancy: 6.2 % / Net I/σ(I): 8.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3JUA Resolution: 2.9→30 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.882 / SU B: 16.507 / SU ML: 0.301 / Cross valid method: THROUGHOUT / ESU R: 0.645 / ESU R Free: 0.35 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 52.28 Å2
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Refinement step | Cycle: 1 / Resolution: 2.9→30 Å
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