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Yorodumi- PDB-4g21: Structural basis for the accommodation of bis- and tris-aromatic ... -
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-Basic information
Entry | Database: PDB / ID: 4g21 | ||||||
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Title | Structural basis for the accommodation of bis- and tris-aromatic derivatives in Vitamin D Nuclear Receptor | ||||||
Components |
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Keywords | transcription/transcription inhibitor / VDR / transcription regulation / nuclear receptor / alpha helical sandwich / ligand / DNA / phosphorylation / nucleus / transcription-transcription inhibitor complex | ||||||
Function / homology | Function and homology information heart jogging / Vitamin D (calciferol) metabolism / SUMOylation of intracellular receptors / vitamin D binding / calcitriol binding / lithocholic acid binding / labyrinthine layer morphogenesis / regulation of thyroid hormone receptor signaling pathway / positive regulation of transcription from RNA polymerase II promoter by galactose / positive regulation of female receptivity ...heart jogging / Vitamin D (calciferol) metabolism / SUMOylation of intracellular receptors / vitamin D binding / calcitriol binding / lithocholic acid binding / labyrinthine layer morphogenesis / regulation of thyroid hormone receptor signaling pathway / positive regulation of transcription from RNA polymerase II promoter by galactose / positive regulation of female receptivity / hematopoietic stem cell proliferation / hypothalamus development / male mating behavior / NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / heart looping / nuclear retinoid X receptor binding / Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 / cellular response to Thyroglobulin triiodothyronine / estrous cycle / Synthesis of bile acids and bile salts / positive regulation of adipose tissue development / peroxisome proliferator activated receptor signaling pathway / Endogenous sterols / Synthesis of bile acids and bile salts via 27-hydroxycholesterol / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / ossification / calcium ion homeostasis / regulation of cellular response to insulin stimulus / response to retinoic acid / histone acetyltransferase activity / Recycling of bile acids and salts / histone acetyltransferase / cellular response to hormone stimulus / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / RORA activates gene expression / positive regulation of neuron differentiation / lactation / Regulation of lipid metabolism by PPARalpha / cerebellum development / BMAL1:CLOCK,NPAS2 activates circadian gene expression / SUMOylation of transcription cofactors / Activation of gene expression by SREBF (SREBP) / nuclear receptor coactivator activity / mRNA transcription by RNA polymerase II / response to progesterone / nuclear receptor binding / hippocampus development / nuclear estrogen receptor binding / RNA polymerase II transcription regulatory region sequence-specific DNA binding / PPARA activates gene expression / Heme signaling / Transcriptional activation of mitochondrial biogenesis / Transcriptional regulation of white adipocyte differentiation / Cytoprotection by HMOX1 / RNA polymerase II transcription regulator complex / cerebral cortex development / nuclear receptor activity / male gonad development / Circadian Clock / response to estradiol / HATs acetylate histones / transcription regulator complex / Estrogen-dependent gene expression / transcription coactivator activity / cell differentiation / protein dimerization activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / positive regulation of apoptotic process / chromatin binding / DNA-templated transcription / positive regulation of DNA-templated transcription / chromatin / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding / nucleoplasm / nucleus / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Danio rerio (zebrafish) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å | ||||||
Authors | Ciesielski, F. / Sato, Y. / Moras, D. / Rochel, N. | ||||||
Citation | Journal: J.Med.Chem. / Year: 2012 Title: Structural basis for the accommodation of bis- and tris-aromatic derivatives in vitamin d nuclear receptor. Authors: Ciesielski, F. / Sato, Y. / Chebaro, Y. / Moras, D. / Dejaegere, A. / Rochel, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4g21.cif.gz | 65.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4g21.ent.gz | 46.5 KB | Display | PDB format |
PDBx/mmJSON format | 4g21.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4g21_validation.pdf.gz | 690 KB | Display | wwPDB validaton report |
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Full document | 4g21_full_validation.pdf.gz | 699.3 KB | Display | |
Data in XML | 4g21_validation.xml.gz | 13.1 KB | Display | |
Data in CIF | 4g21_validation.cif.gz | 16.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g2/4g21 ftp://data.pdbj.org/pub/pdb/validation_reports/g2/4g21 | HTTPS FTP |
-Related structure data
Related structure data | 4g1dC 4g1yC 4g1zC 4g20C 4g2hC 4g2iC 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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Unit cell |
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-Components
#1: Protein | Mass: 33916.543 Da / Num. of mol.: 1 / Fragment: unp residues 156-453 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Danio rerio (zebrafish) / Gene: vdra, nr1i1a, vdr / Plasmid: pET28 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21DE3 / References: UniProt: Q9PTN2 |
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#2: Protein/peptide | Mass: 1776.072 Da / Num. of mol.: 1 / Fragment: unp residues 686-700 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q15788, histone acetyltransferase |
#3: Chemical | ChemComp-0VP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.49 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: Bis-Tris 0.1 M, lithium sulfate 1.6 M and magnesium sulfate 50 mM , pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 |
Detector | Type: ADSC QUANTUM 4r / Detector: CCD / Date: 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.9→20 Å / Num. all: 7344 / Num. obs: 7772 / % possible obs: 98 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
Reflection shell | Resolution: 2.9→2.97 Å / % possible all: 96.1 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.9→20 Å
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