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- PDB-1oj5: Crystal structure of the Nco-A1 PAS-B domain bound to the STAT6 t... -
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Basic information
Entry | Database: PDB / ID: 1oj5 | ||||||
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Title | Crystal structure of the Nco-A1 PAS-B domain bound to the STAT6 transactivation domain LXXLL motif | ||||||
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![]() | TRANSCRIPTIONAL COACTIVATOR / ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() regulation of mast cell proliferation / NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / mammary gland morphogenesis / SUMOylation of transcription cofactors / cellular response to reactive nitrogen species / Recycling of bile acids and salts / negative regulation of type 2 immune response / Synthesis of bile acids and bile salts / positive regulation of isotype switching to IgE isotypes ...regulation of mast cell proliferation / NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / mammary gland morphogenesis / SUMOylation of transcription cofactors / cellular response to reactive nitrogen species / Recycling of bile acids and salts / negative regulation of type 2 immune response / Synthesis of bile acids and bile salts / positive regulation of isotype switching to IgE isotypes / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / Synthesis of bile acids and bile salts via 27-hydroxycholesterol / Endogenous sterols / HATs acetylate histones / T-helper 1 cell lineage commitment / STAT6-mediated induction of chemokines / isotype switching to IgE isotypes / Regulation of lipid metabolism by PPARalpha / Cytoprotection by HMOX1 / interleukin-4-mediated signaling pathway / Estrogen-dependent gene expression / nuclear retinoic acid receptor binding / 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 / mammary gland epithelial cell proliferation / hypothalamus development / male mating behavior / cell surface receptor signaling pathway via JAK-STAT / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Razeto, A. / Ramakrishnan, V. / Giller, K. / Lakomek, N. / Carlomagno, T. / Griesinger, C. / Lodrini, M. / Litterst, C.M. / Pftizner, E. / Becker, S. | ||||||
![]() | ![]() Title: Structure of the Ncoa-1/Src-1 Pas-B Domain Bound to the Lxxll Motif of the Stat6 Transactivation Domain Authors: Razeto, A. / Ramakrishnan, V. / Litterst, C.M. / Giller, K. / Griesinger, C. / Carlomagno, T. / Lakomek, N. / Heimburg, T. / Lodrini, M. / Pfitzner, E. / Becker, S. #1: Journal: J.Biol.Chem. / Year: 2002 Title: An Lxxll Motif in the Transactivation Domain of Stat6 Mediates Recruitment of Ncoa-1/Src-1 Authors: Litterst, C.M. / Pfitzner, E. #2: Journal: J.Biol.Chem. / Year: 2001 Title: Transcriptional Activation by Stat6 Requires the Direct Interaction with Ncoa-1 Authors: Litterst, C.M. / Pfitzner, E. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 40.4 KB | Display | ![]() |
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PDB format | ![]() | 27.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Details | THIS BIOMOLECULE IS A HETERODIMERIC COMPLEX OF A PROTEINCHAIN WITH A PEPTIDE |
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Components
#1: Protein | Mass: 14811.774 Da / Num. of mol.: 1 / Fragment: NCO-A1 PAS-B DOMAIN, RESIDUES 257-385 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
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#2: Protein/peptide | Mass: 1610.865 Da / Num. of mol.: 1 / Fragment: STAT6 LXXLL MOTIF, RESIDUES 795-808 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() | ||||||
#3: Chemical | ChemComp-IOD / ![]() #4: Water | ChemComp-HOH / | ![]() Compound details | ENGINEERED | Sequence details | RESIDUES A254-A256 ARE FROM THE VECTOR PET16BTEV | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | pH: 7 / Details: 20 % PEG3350, 0.2 M LICL, pH 7.00 | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 24, 2003 / Details: OSMIC MIRRORS CMF12-38CU6 |
Radiation | Monochromator: OSMIC MIRRORS CMF12-38CU6 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.21→19.21 Å / Num. obs: 8138 / % possible obs: 99.7 % / Redundancy: 16.8 % / Biso Wilson estimate: 28.7 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 29.9 |
Reflection shell | Resolution: 2.21→2.25 Å / Redundancy: 16 % / Rmerge(I) obs: 0.3254 / Mean I/σ(I) obs: 8.71 / % possible all: 98.1 |
Reflection | *PLUS Highest resolution: 2.21 Å / Lowest resolution: 19.2 Å / Redundancy: 16.8 % / Num. measured all: 137915 / Rmerge(I) obs: 0.089 |
Reflection shell | *PLUS % possible obs: 98.1 % / Redundancy: 16 % / Rmerge(I) obs: 0.325 / Mean I/σ(I) obs: 8.7 |
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Processing
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Refinement | Method to determine structure![]() Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE LAST RUN OF REFINEMENT WAS PERFORMED WITH ALL THE REFLECTIONS. THE R FREE REPORTED ABOVE IS REFERRED TO THE PREVIOUS RUN OF REFINEMENT. ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THE LAST RUN OF REFINEMENT WAS PERFORMED WITH ALL THE REFLECTIONS. THE R FREE REPORTED ABOVE IS REFERRED TO THE PREVIOUS RUN OF REFINEMENT. SIDE CHAINS WITH POOR ELECTRON DENSITY WERE ASSIGNED OCCUPANCY 0.5
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.92 Å2
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Refinement step | Cycle: LAST / Resolution: 2.21→19.21 Å
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Refine LS restraints |
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