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Yorodumi- PDB-4bs2: NMR structure of human TDP-43 tandem RRMs in complex with UG-rich RNA -
+Open data
-Basic information
Entry | Database: PDB / ID: 4bs2 | ||||||
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Title | NMR structure of human TDP-43 tandem RRMs in complex with UG-rich RNA | ||||||
Components |
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Keywords | TRANSCRIPTION / HNRNP / CYSTIC FIBROSIS / NEURODEGENERATION / ISOTOPE-LABELLED RNA / HAMMERHEAD RIBOZYME | ||||||
Function / homology | Function and homology information nuclear inner membrane organization / interchromatin granule / perichromatin fibrils / 3'-UTR-mediated mRNA destabilization / 3'-UTR-mediated mRNA stabilization / intracellular non-membrane-bounded organelle / negative regulation by host of viral transcription / pre-mRNA intronic binding / molecular condensate scaffold activity / response to endoplasmic reticulum stress ...nuclear inner membrane organization / interchromatin granule / perichromatin fibrils / 3'-UTR-mediated mRNA destabilization / 3'-UTR-mediated mRNA stabilization / intracellular non-membrane-bounded organelle / negative regulation by host of viral transcription / pre-mRNA intronic binding / molecular condensate scaffold activity / response to endoplasmic reticulum stress / RNA splicing / negative regulation of protein phosphorylation / mRNA 3'-UTR binding / regulation of protein stability / regulation of circadian rhythm / positive regulation of insulin secretion / mRNA processing / cytoplasmic stress granule / positive regulation of protein import into nucleus / rhythmic process / double-stranded DNA binding / regulation of gene expression / regulation of apoptotic process / amyloid fibril formation / regulation of cell cycle / nuclear speck / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of gene expression / lipid binding / mitochondrion / DNA binding / RNA binding / nucleoplasm / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING, MOLECULAR DYNAMICS IN TORSION ANGLE SPACE | ||||||
Authors | Lukavsky, P.J. / Daujotyte, D. / Tollervey, J.R. / Ule, J. / Stuani, C. / Buratti, E. / Baralle, F.E. / Damberger, F.F. / Allain, F.H.T. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2013 Title: Molecular Basis of Ug-Rich RNA Recognition by the Human Splicing Factor Tdp-43 Authors: Lukavsky, P.J. / Daujotyte, D. / Tollervey, J.R. / Ule, J. / Stuani, C. / Buratti, E. / Baralle, F.E. / Damberger, F.F. / Allain, F.H.T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4bs2.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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PDB format | pdb4bs2.ent.gz | 1.2 MB | Display | PDB format |
PDBx/mmJSON format | 4bs2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bs/4bs2 ftp://data.pdbj.org/pub/pdb/validation_reports/bs/4bs2 | 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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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 19995.734 Da / Num. of mol.: 1 / Fragment: RNA BINDING DOMAIN, RESIDUES 102-269 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): RIL / References: UniProt: Q13148 |
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#2: RNA chain | Mass: 3877.352 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: MEASUREMENTS WERE PERFORMED ON THREE DIFFERENT SAMPLES,15N -LABELLED TDP-43 WITH UNLABELLED RNA, 13C,15N- LABELLED TDP-43 WITH UNLABELLED RNA, 15N-LABELLED TDP-43 WITH 13C,15N-LABELLED RNA |
-Sample preparation
Details | Contents: 94%WATER/6%D2O |
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Sample conditions | Ionic strength: 50 mM / pH: 6.8 / Temperature: 298.0 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 900 MHz |
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-Processing
NMR software |
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Refinement | Method: SIMULATED ANNEALING, MOLECULAR DYNAMICS IN TORSION ANGLE SPACE Software ordinal: 1 | |||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY AND RESTRAINT VIOLATION Conformers calculated total number: 50 / Conformers submitted total number: 20 |