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Yorodumi- PDB-1x0f: Complex structure of the C-terminal RNA-binding domain of hnRNP D... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1x0f | ||||||
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| Title | Complex structure of the C-terminal RNA-binding domain of hnRNP D(AUF1) with telomeric DNA | ||||||
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Keywords | TRANSCRIPTION/DNA / RNA-binding domain / DNA-binding domain / RRM / hnRNP D / AUF1 / Telomere / Complex / structural genomics / TRANSCRIPTION-DNA COMPLEX | ||||||
| Function / homology | Function and homology informationhepatocyte dedifferentiation / cellular response to putrescine / circadian regulation of translation / response to rapamycin / mCRD-mediated mRNA stability complex / negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CRD-mediated mRNA stabilization / response to sodium phosphate / 3'-UTR-mediated mRNA destabilization / positive regulation of telomere capping ...hepatocyte dedifferentiation / cellular response to putrescine / circadian regulation of translation / response to rapamycin / mCRD-mediated mRNA stability complex / negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CRD-mediated mRNA stabilization / response to sodium phosphate / 3'-UTR-mediated mRNA destabilization / positive regulation of telomere capping / mRNA 3'-UTR AU-rich region binding / positive regulation of cytoplasmic translation / RNA catabolic process / telomeric DNA binding / minor groove of adenine-thymine-rich DNA binding / Processing of Capped Intron-Containing Pre-mRNA / response to electrical stimulus / RNA processing / positive regulation of telomere maintenance via telomerase / cellular response to nitric oxide / mRNA Splicing - Major Pathway / positive regulation of translation / cerebellum development / AUF1 (hnRNP D0) binds and destabilizes mRNA / cellular response to amino acid stimulus / cellular response to estradiol stimulus / liver development / regulation of circadian rhythm / response to calcium ion / histone deacetylase binding / regulation of gene expression / postsynaptic density / ribonucleoprotein complex / chromatin binding / regulation of DNA-templated transcription / chromatin / positive regulation of DNA-templated transcription / glutamatergic synapse / positive regulation of transcription by RNA polymerase II / RNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Enokizono, Y. / Konishi, Y. / Nagata, K. / Ouhashi, K. / Uesugi, S. / Ishikawa, F. / Katahira, M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2005Title: Structure of hnRNP D complexed with single-stranded telomere DNA and unfolding of the quadruplex by heterogeneous nuclear ribonucleoprotein D. Authors: Enokizono, Y. / Konishi, Y. / Nagata, K. / Ouhashi, K. / Uesugi, S. / Ishikawa, F. / Katahira, M. #1: Journal: J.Biol.Chem. / Year: 2005Title: Structure of hnRNP D complexed with single-stranded telomere DNA and unfolding of the quadruplex by hnRNP D Authors: Enokizono, Y. / Konishi, Y. / Nagata, K. / Ouhashi, K. / Uesugi, S. / Ishikawa, F. / Katahira, M. #2: Journal: J.Mol.Biol. / Year: 2001Title: Structure of the C-terminal RNA-binding domain of hnRNP D0 (AUF1), its interactions with RNA and DNA, and change in backbone dynamics upon complex formation with DNA Authors: Katahira, M. / Miyanoiri, Y. / Enokizono, Y. / Matsuda, G. / Nagata, T. / Ishikawa, F. / Uesugi, S. #3: Journal: J.Mol.Biol. / Year: 1999Title: Structure and interactions with RNA of the N-terminal UUAG-specific RNA-binding domain of hnRNP D0 Authors: Nagata, T. / Kurihara, Y. / Matsuda, G. / Saeki, J. / Kohno, T. / Yanagida, Y. / Ishikawa, F. / Uesugi, S. / Katahira, M. #4: Journal: Mol.Cell.Biol. / Year: 1993 Title: Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n Authors: Ishikawa, F. / Matunis, M.J. / Dreyfuss, G. / Cech, T.R. | ||||||
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| Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED | ||||||
| Remark 700 | SHEET DETERMINATION METHOD: AUTHOR DETERMINED |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1x0f.cif.gz | 550.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1x0f.ent.gz | 461.3 KB | Display | PDB format |
| PDBx/mmJSON format | 1x0f.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1x0f_validation.pdf.gz | 348.1 KB | Display | wwPDB validaton report |
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| Full document | 1x0f_full_validation.pdf.gz | 593.5 KB | Display | |
| Data in XML | 1x0f_validation.xml.gz | 81.2 KB | Display | |
| Data in CIF | 1x0f_validation.cif.gz | 108 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x0/1x0f ftp://data.pdbj.org/pub/pdb/validation_reports/x0/1x0f | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: DNA chain | Mass: 1230.854 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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| #2: Protein | Mass: 9103.628 Da / Num. of mol.: 1 / Fragment: C-terminal RNA-binding domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET3a / Species (production host): Escherichia coli / Production host: ![]() |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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| NMR experiment |
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| NMR details | Text: This structure was determined using 2D homonuclear and 3D heteronuclear techniques. |
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Sample preparation
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| Sample conditions | Ionic strength: 100mM NaCl / pH: 6 / Pressure: 1 atm / Temperature: 288 K |
-NMR measurement
| NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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Processing
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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: 228 / Conformers submitted total number: 20 |
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