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- PDB-1t5z: Crystal Structure of the Androgen Receptor Ligand Binding Domain ... -

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Basic information

Entry
Database: PDB / ID: 1t5z
TitleCrystal Structure of the Androgen Receptor Ligand Binding Domain (LBD) with DHT and a peptide derived from its physiological coactivator ARA70
Components
  • Androgen receptor
  • Nuclear receptor coactivator 4
KeywordsHORMONE/GROWTH FACTOR / androgen receptor ligand binding domain ARA70 crystal structure coactivators / HORMONE-GROWTH FACTOR COMPLEX
Function / homology
Function and homology information


male somatic sex determination / lateral sprouting involved in mammary gland duct morphogenesis / male genitalia morphogenesis / POU domain binding / negative regulation of integrin biosynthetic process / regulation of developmental growth / positive regulation of integrin biosynthetic process / intracellular receptor signaling pathway / tertiary branching involved in mammary gland duct morphogenesis / animal organ formation ...male somatic sex determination / lateral sprouting involved in mammary gland duct morphogenesis / male genitalia morphogenesis / POU domain binding / negative regulation of integrin biosynthetic process / regulation of developmental growth / positive regulation of integrin biosynthetic process / intracellular receptor signaling pathway / tertiary branching involved in mammary gland duct morphogenesis / animal organ formation / regulation of prostatic bud formation / androgen binding / regulation of systemic arterial blood pressure / Leydig cell differentiation / 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 / prostate gland epithelium morphogenesis / protein targeting to lysosome / cellular response to testosterone stimulus / membraneless organelle assembly / 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 / morphogenesis of an epithelial fold / cellular response to steroid hormone stimulus / seminiferous tubule development / RUNX2 regulates osteoblast differentiation / autolysosome / androgen receptor signaling pathway / mammary gland alveolus development / single fertilization / cellular response to estrogen stimulus / estrogen response element binding / nuclear receptor-mediated steroid hormone signaling pathway / positive regulation of phosphorylation / regulation of protein localization to plasma membrane / RNA polymerase II core promoter sequence-specific DNA binding / estrogen receptor signaling pathway / response to hormone / steroid binding / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / autophagosome / insulin-like growth factor receptor signaling pathway / epithelial cell proliferation / negative regulation of extrinsic apoptotic signaling pathway / positive regulation of cell differentiation / SUMOylation of intracellular receptors / transcription coactivator binding / molecular condensate scaffold activity / G protein-coupled receptor activity / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / multicellular organism growth / beta-catenin binding / positive regulation of miRNA transcription / Nuclear Receptor transcription pathway / 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 / chromosome / ATPase binding / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / DNA-binding transcription activator activity, RNA polymerase II-specific / cytoplasmic vesicle / spermatogenesis / molecular adaptor activity / RNA polymerase II-specific DNA-binding transcription factor binding / in utero embryonic development / intracellular iron ion homeostasis / transcription by RNA polymerase II / transcription coactivator activity / positive regulation of MAPK cascade / DNA-binding transcription factor activity, RNA polymerase II-specific / transcription cis-regulatory region binding / Ub-specific processing proteases / nuclear speck / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of cell population proliferation / signaling receptor binding / positive regulation of cell population proliferation / positive regulation of gene expression / chromatin binding / chromatin / positive regulation of DNA-templated transcription / enzyme binding / negative regulation of transcription by RNA polymerase II / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding / nucleoplasm / nucleus / plasma membrane / cytosol
Similarity search - Function
Nuclear coactivator / Nuclear receptor coactivator 4 / Nuclear coactivator / Androgen receptor / Androgen receptor / : / Retinoid X Receptor / Retinoid X Receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type ...Nuclear coactivator / Nuclear receptor coactivator 4 / Nuclear coactivator / Androgen receptor / Androgen receptor / : / Retinoid X Receptor / Retinoid X Receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Double treble clef zinc finger, C4 type / Nuclear hormone receptors DNA-binding domain profile. / c4 zinc finger in nuclear hormone receptors / Nuclear hormone receptor, ligand-binding domain / Nuclear hormone receptor-like domain superfamily / Ligand-binding domain of nuclear hormone receptor / Nuclear receptor (NR) ligand-binding (LBD) domain profile. / Ligand binding domain of hormone receptors / Zinc finger, NHR/GATA-type / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
5-ALPHA-DIHYDROTESTOSTERONE / Androgen receptor / Nuclear receptor coactivator 4
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsEstebanez-Perpina, E. / Moore, J.M.R. / Mar, E. / Nguyen, P. / Delgado-Rodrigues, E. / Baxter, J.D. / Webb, P. / Fletterick, R.J. / Guy, R.K.
CitationJournal: J.Biol.Chem. / Year: 2005
Title: The Molecular Mechanisms of Coactivator Utilization in Ligand-dependent Transactivation by the Androgen Receptor.
Authors: Estebanez-Perpina, E. / Moore, J.M.R. / Mar, E. / Delgado-Rodrigues, E. / Nguyen, P. / Baxter, J.D. / Buehrer, B.M. / Webb, P. / Fletterick, R.J. / Guy, R.K.
History
DepositionMay 5, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 25, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 14, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Androgen receptor
B: Nuclear receptor coactivator 4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,4613
Polymers31,1702
Non-polymers2901
Water1,56787
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1820 Å2
ΔGint-13 kcal/mol
Surface area12320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)55.680, 66.423, 68.253
Angle α, β, γ (deg.)90, 90, 90
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Androgen receptor / Dihydrotestosterone receptor


Mass: 29277.340 Da / Num. of mol.: 1 / Fragment: AR Ligand Binding Domain 669-918
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AR, NR3C4, DHTR / Production host: Escherichia coli (E. coli) / References: UniProt: P10275
#2: Protein/peptide Nuclear receptor coactivator 4 / NCoA-4 / 70 kDa androgen receptor coactivator / 70 kDa AR-activator / Ret-activating protein ELE1


Mass: 1893.124 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: NCOA4, ARA70, RFG, ELE1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q13772
#3: Chemical ChemComp-DHT / 5-ALPHA-DIHYDROTESTOSTERONE


Mass: 290.440 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C19H30O2 / Comment: hormone*YM
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 87 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.104 Å3/Da / Density % sol: 41.58 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: Hepes, Na-citrate, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.1 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 2, 2003
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
ReflectionResolution: 2.3→24 Å / Num. all: 10881 / Num. obs: 10881 / % possible obs: 82.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5 % / Biso Wilson estimate: 9.8 Å2 / Rsym value: 0.011 / Net I/σ(I): 5.1
Reflection shellHighest resolution: 2.3 Å / % possible all: 90

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Processing

Software
NameClassification
DENZOdata reduction
SCALEPACKdata scaling
CNSrefinement
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3→24 Å / Isotropic thermal model: anisotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.26 1468 -RANDOM
Rwork0.228 ---
all-10881 --
obs-10881 90 %-
Displacement parametersBiso mean: 38.9 Å2
Baniso -1Baniso -2Baniso -3
1-25.47 Å20 Å20 Å2
2---14.83 Å20 Å2
3----10.64 Å2
Refine analyzeLuzzati coordinate error obs: 0.35 Å / Luzzati d res low obs: 5 Å / Luzzati sigma a obs: 0.63 Å
Refinement stepCycle: LAST / Resolution: 2.3→24 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2141 0 21 87 2249
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_dihedral_angle_d19.1
X-RAY DIFFRACTIONc_improper_angle_d0.77

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