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Yorodumi- PDB-1kv6: X-ray structure of the orphan nuclear receptor ERR3 ligand-bindin... -
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-Basic information
Entry | Database: PDB / ID: 1kv6 | ||||||
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Title | X-ray structure of the orphan nuclear receptor ERR3 ligand-binding domain in the constitutively active conformation | ||||||
Components |
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Keywords | GENE REGULATION / transcriptionally active conformation in absence of ligand / Structural Proteomics in Europe / SPINE / Structural Genomics | ||||||
Function / homology | Function and homology information regulation of cellular response to drug / nuclear progesterone receptor binding / nuclear receptor binding => GO:0016922 / : / AF-2 domain binding / : / chromatin => GO:0000785 / bile acid and bile salt transport / labyrinthine layer morphogenesis / regulation of thyroid hormone mediated signaling pathway ...regulation of cellular response to drug / nuclear progesterone receptor binding / nuclear receptor binding => GO:0016922 / : / AF-2 domain binding / : / chromatin => GO:0000785 / bile acid and bile salt transport / labyrinthine layer morphogenesis / regulation of thyroid hormone mediated signaling pathway / positive regulation of transcription from RNA polymerase II promoter by galactose / positive regulation of female receptivity / nuclear steroid receptor activity / hypothalamus development / male mating behavior / NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / aryl hydrocarbon receptor binding / regulation of lipid metabolic process / estrous cycle / cellular response to Thyroglobulin triiodothyronine / Synthesis of bile acids and bile salts / retinoic acid receptor signaling pathway / estrogen response element binding / Endogenous sterols / Synthesis of bile acids and bile salts via 27-hydroxycholesterol / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / nuclear retinoid X receptor binding / intracellular steroid hormone receptor signaling pathway / response to retinoic acid / histone acetyltransferase activity / regulation of cellular response to insulin stimulus / Recycling of bile acids and salts / histone acetyltransferase / cellular response to hormone stimulus / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / positive regulation of adipose tissue development / peroxisome proliferator activated receptor signaling pathway / RORA activates gene expression / lactation / steroid binding / positive regulation of neuron differentiation / Regulation of lipid metabolism by PPARalpha / cerebellum development / BMAL1:CLOCK,NPAS2 activates circadian gene expression / Activation of gene expression by SREBF (SREBP) / SUMOylation of transcription cofactors / nuclear receptor coactivator activity / response to progesterone / nuclear estrogen receptor binding / nuclear receptor binding / hippocampus development / RNA polymerase II transcription regulatory region sequence-specific DNA binding / Heme signaling / mRNA transcription by RNA polymerase II / Transcriptional activation of mitochondrial biogenesis / PPARA activates gene expression / Cytoprotection by HMOX1 / cerebral cortex development / Transcriptional regulation of white adipocyte differentiation / Nuclear Receptor transcription pathway / RNA polymerase II transcription regulator complex / male gonad development / nuclear receptor activity / Circadian Clock / sequence-specific double-stranded DNA binding / response to estradiol / positive regulation of cold-induced thermogenesis / HATs acetylate histones / DNA-binding transcription activator activity, RNA polymerase II-specific / Estrogen-dependent gene expression / transcription regulator complex / transcription coactivator activity / protein dimerization activity / DNA-binding transcription factor activity, RNA polymerase II-specific / neuron projection / positive regulation of apoptotic process / chromatin binding / chromatin / protein-containing complex binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / enzyme binding / positive regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding / nucleoplasm / identical protein binding / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Greschik, H. / Wurtz, J.-M. / Sanglier, S. / Bourguet, W. / van Dorsselaer, A. / Moras, D. / Renaud, J.-P. / Structural Proteomics in Europe (SPINE) | ||||||
Citation | Journal: Mol.Cell / Year: 2002 Title: Structural and Functional Evidence for Ligand-Independent Transcriptional Activation by the Estrogen-Related Receptor 3 Authors: Greschik, H. / Wurtz, J.-M. / Sanglier, S. / Bourguet, W. / van Dorsselaer, A. / Moras, D. / Renaud, J.-P. #1: Journal: Nature / Year: 1997 Title: Molecular basis of agonism and antagonism in the oestrogen receptor Authors: Brzozowski, A.M. / Pike, A.C. / Dauter, Z. / Hubbard, R.E. / Bonn, T. / Engstrom, O. / Ohman, L. / Greene, G.L. / Gustafsson, J.A. #2: Journal: Cell(Cambridge,Mass.) / Year: 1998 Title: The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction with tamoxifen Authors: Shiau, A.K. / Barstad, D. / Loria, P.M. / Cheng, L. / Agard, D.A. / Greene, G.L. #3: Journal: Embo J. / Year: 2001 Title: X-ray structure of the orphan nuclear receptor RORbeta ligand-binding domain in the active conformation Authors: Stehlin, C. / Wurtz, J.M. / Steinmetz, A. / Greiner, E. / Schuele, R. / Moras, D. / Renaud, J.P. #4: Journal: Cell.Mol.Life Sci. / Year: 2000 Title: Structural studies on nuclear receptors Authors: Renaud, J.P. / Moras, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kv6.cif.gz | 103 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1kv6.ent.gz | 79.5 KB | Display | PDB format |
PDBx/mmJSON format | 1kv6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kv/1kv6 ftp://data.pdbj.org/pub/pdb/validation_reports/kv/1kv6 | HTTPS FTP |
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-Related structure data
Related structure data | 3erdS S: Starting model for refinement |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 26084.373 Da / Num. of mol.: 2 / Fragment: ligand-binding domain Source method: isolated from a genetically manipulated source Details: complex with a SRC1 coactivator peptide in the absence of ligand Source: (gene. exp.) Homo sapiens (human) / Gene: NR3B3 / Plasmid: pET-15b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P62508 #2: Protein/peptide | Mass: 1776.072 Da / Num. of mol.: 2 / Fragment: second NR-box / Source method: obtained synthetically / Details: This sequence occurs naturally in humans / References: UniProt: Q13420, UniProt: Q15788*PLUS #3: 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: 4.04 Å3/Da / Density % sol: 69.3 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8 Details: Tris.HCl, ammonium sulfate, glycerol, pH 8.0, VAPOR DIFFUSION, HANGING DROP at 277K | ||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 60 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 130 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jan 27, 2001 / Details: diamond(111) monochromator, Ge(220) focusing |
Radiation | Monochromator: diamond(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→15 Å / Num. obs: 23306 / % possible obs: 96.7 % / Biso Wilson estimate: 71 Å2 / Rsym value: 0.049 |
Reflection shell | Resolution: 2.7→2.81 Å / Num. unique all: 2587 / Rsym value: 0.148 / % possible all: 99.1 |
Reflection | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 15 Å / Rmerge(I) obs: 0.049 |
Reflection shell | *PLUS Rmerge(I) obs: 0.148 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PBD ENTRY 3ERD Resolution: 2.7→15 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.7→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.7→2.75 Å
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Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 15 Å / % reflection Rfree: 5 % / Rfactor Rfree: 0.267 / Rfactor Rwork: 0.233 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |