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Yorodumi- PDB-2rt5: Structural insights into the recruitment of SMRT by the co-repres... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2rt5 | ||||||
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Title | Structural insights into the recruitment of SMRT by the co-repressor SHARP under phosphorylative regulation | ||||||
Components |
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Keywords | TRANSCRIPTION REGULATOR / SHARP / SPOC domain / SMRT / phosphorylation | ||||||
Function / homology | Function and homology information Loss of MECP2 binding ability to the NCoR/SMRT complex / random inactivation of X chromosome / regulatory ncRNA-mediated heterochromatin formation / negative regulation of androgen receptor signaling pathway / regulation of ketone metabolic process / nuclear glucocorticoid receptor binding / Notch binding / RHOBTB1 GTPase cycle / positive regulation of neurogenesis / : ...Loss of MECP2 binding ability to the NCoR/SMRT complex / random inactivation of X chromosome / regulatory ncRNA-mediated heterochromatin formation / negative regulation of androgen receptor signaling pathway / regulation of ketone metabolic process / nuclear glucocorticoid receptor binding / Notch binding / RHOBTB1 GTPase cycle / positive regulation of neurogenesis / : / NR1H2 & NR1H3 regulate gene expression to control bile acid homeostasis / Notch-HLH transcription pathway / Regulation of MECP2 expression and activity / estrous cycle / nuclear retinoid X receptor binding / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / Notch signaling pathway / lactation / transcription repressor complex / Regulation of lipid metabolism by PPARalpha / cerebellum development / negative regulation of miRNA transcription / SUMOylation of transcription cofactors / HDACs deacetylate histones / Downregulation of SMAD2/3:SMAD4 transcriptional activity / PPARA activates gene expression / Cytoprotection by HMOX1 / NOTCH1 Intracellular Domain Regulates Transcription / histone deacetylase binding / Transcriptional regulation of white adipocyte differentiation / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / Nuclear Receptor transcription pathway / nuclear matrix / HCMV Early Events / transcription corepressor activity / response to estradiol / RNA polymerase II-specific DNA-binding transcription factor binding / nuclear body / negative regulation of DNA-templated transcription / mRNA binding / chromatin binding / chromatin / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / DNA binding / RNA binding / extracellular exosome / nucleoplasm / membrane / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Mikami, S. / Kanaba, T. / Mishima, M. | ||||||
Citation | Journal: Structure / Year: 2014 Title: Structural insights into the recruitment of SMRT by the corepressor SHARP under phosphorylative regulation. Authors: Mikami, S. / Kanaba, T. / Takizawa, N. / Kobayashi, A. / Maesaki, R. / Fujiwara, T. / Ito, Y. / Mishima, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rt5.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2rt5.ent.gz | 900.2 KB | Display | PDB format |
PDBx/mmJSON format | 2rt5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2rt5_validation.pdf.gz | 418.5 KB | Display | wwPDB validaton report |
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Full document | 2rt5_full_validation.pdf.gz | 693.7 KB | Display | |
Data in XML | 2rt5_validation.xml.gz | 84.9 KB | Display | |
Data in CIF | 2rt5_validation.cif.gz | 106.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rt/2rt5 ftp://data.pdbj.org/pub/pdb/validation_reports/rt/2rt5 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 18471.402 Da / Num. of mol.: 1 / Fragment: SPOC domain, residues 3496-3664 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SHARP / Production host: Escherichia coli (E. coli) / References: UniProt: Q96T58 |
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#2: Protein/peptide | Mass: 1102.880 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q9Y618 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Solvent system: 93% H2O/7% D2O |
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Sample conditions | Ionic strength: 0 / pH: 7.5 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software | Name: CNS / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |