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Yorodumi- PDB-1xow: Crystal structure of the human androgen receptor ligand binding d... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1xow | ||||||
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Title | Crystal structure of the human androgen receptor ligand binding domain bound with an androgen receptor NH2-terminal peptide, AR20-30, and R1881 | ||||||
Components |
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Keywords | TRANSCRIPTION / crystal structure / human androgen receptor ligand binding domain / androgen receptor NH2-terminal peptide AR20-30 / R1881 | ||||||
Function / homology | Function and homology information male somatic sex determination / : / lateral sprouting involved in mammary gland duct morphogenesis / POU domain binding / negative regulation of integrin biosynthetic process / regulation of developmental growth / male genitalia morphogenesis / positive regulation of integrin biosynthetic process / intracellular receptor signaling pathway / tertiary branching involved in mammary gland duct morphogenesis ...male somatic sex determination / : / lateral sprouting involved in mammary gland duct morphogenesis / POU domain binding / negative regulation of integrin biosynthetic process / regulation of developmental growth / male genitalia morphogenesis / positive regulation of integrin biosynthetic process / intracellular receptor signaling pathway / tertiary branching involved in mammary gland duct morphogenesis / animal organ formation / androgen binding / Leydig cell differentiation / regulation of systemic arterial blood pressure / epithelial cell morphogenesis / prostate gland growth / epithelial cell differentiation involved in prostate gland development / positive regulation of epithelial cell proliferation involved in prostate gland development / membraneless organelle assembly / prostate gland epithelium morphogenesis / cellular response to testosterone stimulus / RNA polymerase II general transcription initiation factor binding / positive regulation of insulin-like growth factor receptor signaling pathway / positive regulation of intracellular estrogen receptor signaling pathway / positive regulation of transcription by RNA polymerase III / cellular response to steroid hormone stimulus / morphogenesis of an epithelial fold / seminiferous tubule development / androgen receptor signaling pathway / RUNX2 regulates osteoblast differentiation / single fertilization / mammary gland alveolus development / regulation of protein localization to plasma membrane / cellular response to estrogen stimulus / estrogen response element binding / nuclear receptor-mediated steroid hormone signaling pathway / positive regulation of phosphorylation / estrogen receptor signaling pathway / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / steroid binding / insulin-like growth factor receptor signaling pathway / epithelial cell proliferation / negative regulation of extrinsic apoptotic signaling pathway / positive regulation of cell differentiation / G protein-coupled receptor activity / SUMOylation of intracellular receptors / molecular condensate scaffold activity / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / multicellular organism growth / transcription coactivator binding / positive regulation of miRNA transcription / Nuclear Receptor transcription pathway / beta-catenin binding / nuclear receptor activity / male gonad development / negative regulation of epithelial cell proliferation / MAPK cascade / cell-cell signaling / positive regulation of NF-kappaB transcription factor activity / ATPase binding / DNA-binding transcription activator activity, RNA polymerase II-specific / spermatogenesis / RNA polymerase II-specific DNA-binding transcription factor binding / in utero embryonic development / transcription by RNA polymerase II / positive regulation of MAPK cascade / molecular adaptor activity / transcription cis-regulatory region binding / DNA-binding transcription factor activity, RNA polymerase II-specific / Ub-specific processing proteases / nuclear speck / DNA-binding transcription factor activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of cell population proliferation / signaling receptor binding / chromatin binding / positive regulation of cell population proliferation / positive regulation of gene expression / chromatin / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / enzyme binding / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.8 Å | ||||||
Authors | He, B. / Gampe Jr., R.T. / Kole, A.J. / Hnat, A.T. / Stanley, T.B. / An, G. / Stewart, E.L. / Kalman, R.I. / Minges, J.T. / Wilson, E.M. | ||||||
Citation | Journal: Mol.Cell / Year: 2004 Title: Structural basis for androgen receptor interdomain and coactivator interactions suggests a transition in nuclear receptor activation function dominance Authors: He, B. / Gampe Jr., R.T. / Kole, A.J. / Hnat, A.T. / Stanley, T.B. / An, G. / Stewart, E.L. / Kalman, R.I. / Minges, J.T. / Wilson, E.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1xow.cif.gz | 69.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1xow.ent.gz | 50.4 KB | Display | PDB format |
PDBx/mmJSON format | 1xow.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1xow_validation.pdf.gz | 704.1 KB | Display | wwPDB validaton report |
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Full document | 1xow_full_validation.pdf.gz | 706 KB | Display | |
Data in XML | 1xow_validation.xml.gz | 14 KB | Display | |
Data in CIF | 1xow_validation.cif.gz | 19.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xo/1xow ftp://data.pdbj.org/pub/pdb/validation_reports/xo/1xow | HTTPS FTP |
-Related structure data
Related structure data | 1xq3C 2ao6C 1i37S 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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Unit cell |
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-Components
#1: Protein | Mass: 29046.074 Da / Num. of mol.: 1 / Fragment: ligand binding domain Source method: isolated from a genetically manipulated source Details: inhibited by r1881 / Source: (gene. exp.) Homo sapiens (human) / Gene: Ar, Nr3c4 / Plasmid: pET15b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21DE3 / References: UniProt: P10275 |
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#2: Protein/peptide | Mass: 1267.413 Da / Num. of mol.: 1 / Fragment: N-terminal FXXLF domain / Source method: obtained synthetically Details: decapeptide of human AR NH2-terminal residues 20-30 References: UniProt: P10275 |
#3: Chemical | ChemComp-R18 / ( |
#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: 2.02 Å3/Da / Density % sol: 38.5 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 100mM BTP, 0.6-1.2M Li2SO4, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 26, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. all: 22123 / Num. obs: 22123 / % possible obs: 90.4 % / Observed criterion σ(I): 0 / Biso Wilson estimate: 31 Å2 / Rmerge(I) obs: 0.041 / Net I/σ(I): 37.8 |
Reflection shell | Resolution: 1.8→1.86 Å / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 2 / Num. unique all: 1011 / % possible all: 42 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1I37 Resolution: 1.8→22 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 1404666.74 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 53.0545 Å2 / ksol: 0.383466 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.8→22 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.91 Å / Rfactor Rfree error: 0.033 / Total num. of bins used: 6
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Xplor file |
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