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Yorodumi- PDB-2k7l: NMR structure of a complex formed by the C-terminal domain of hum... -
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-Basic information
Entry | Database: PDB / ID: 2k7l | ||||||
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Title | NMR structure of a complex formed by the C-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1 | ||||||
Components |
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Keywords | TRANSCRIPTION / TFIIF / FCP1 / phosphorylation / CK2 / RAP74 / Nucleus / Phosphoprotein / Polymorphism / Transcription regulation | ||||||
Function / homology | Function and homology information RNA polymerase II CTD heptapeptide repeat phosphatase activity / negative regulation of cell growth involved in cardiac muscle cell development / Tat protein binding / phosphatase activator activity / TFIIF-class transcription factor complex binding / transcription factor TFIIF complex / exit from mitosis / positive regulation by host of viral transcription / Abortive elongation of HIV-1 transcript in the absence of Tat / FGFR2 alternative splicing ...RNA polymerase II CTD heptapeptide repeat phosphatase activity / negative regulation of cell growth involved in cardiac muscle cell development / Tat protein binding / phosphatase activator activity / TFIIF-class transcription factor complex binding / transcription factor TFIIF complex / exit from mitosis / positive regulation by host of viral transcription / Abortive elongation of HIV-1 transcript in the absence of Tat / FGFR2 alternative splicing / RNA polymerase II general transcription initiation factor binding / Viral Messenger RNA Synthesis / Signaling by FGFR2 IIIa TM / myosin phosphatase activity / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / RNA polymerase II general transcription initiation factor activity / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / transcription factor TFIID complex / mRNA Capping / mRNA Splicing - Minor Pathway / protein-serine/threonine phosphatase / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / phosphoprotein phosphatase activity / Processing of Capped Intron-Containing Pre-mRNA / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / RNA polymerase II transcribes snRNA genes / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / spindle midzone / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / mRNA Splicing - Major Pathway / protein dephosphorylation / transcription elongation by RNA polymerase II / promoter-specific chromatin binding / transcription initiation at RNA polymerase II promoter / negative regulation of protein binding / TP53 Regulates Transcription of DNA Repair Genes / positive regulation of transcription elongation by RNA polymerase II / response to virus / spindle / spindle pole / cell junction / midbody / protein phosphatase binding / Estrogen-dependent gene expression / transcription by RNA polymerase II / protein domain specific binding / cell division / intracellular membrane-bounded organelle / centrosome / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / RNA binding / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model type details | minimized average | ||||||
Authors | Yang, A. / Abbott, K.L. / Desjardins, A. / Di Lello, P. / Omichinski, J.G. / Legault, P. | ||||||
Citation | Journal: Biochemistry / Year: 2009 Title: NMR structure of a complex formed by the carboxyl-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1 phosphatase Authors: Yang, A. / Abbott, K.L. / Desjardins, A. / Di Lello, P. / Omichinski, J.G. / Legault, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2k7l.cif.gz | 595.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2k7l.ent.gz | 519.5 KB | Display | PDB format |
PDBx/mmJSON format | 2k7l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k7/2k7l ftp://data.pdbj.org/pub/pdb/validation_reports/k7/2k7l | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2398.470 Da / Num. of mol.: 1 / Fragment: C-terminal domain (UNP residues 451 to 517) / Source method: obtained synthetically Details: The peptide was chemically synthesized by the solid-phase method References: UniProt: Q9Y5B0*PLUS |
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#2: Protein | Mass: 7906.295 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GTF2F1, RAP74 / Production host: Escherichia coli (E. coli) / Strain (production host): Topp2 / References: UniProt: P35269 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 10-40 / pH: 6.5 / Pressure: ambient / Temperature: 300 K |
-NMR measurement
NMR spectrometer | Type: Varian Unity / Manufacturer: Varian / Model: UNITY / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 21 / Conformers submitted total number: 21 |