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Yorodumi- PDB-2kt5: RRM domain of mRNA export adaptor REF2-I bound to HSV-1 ICP27 peptide -
+Open data
-Basic information
Entry | Database: PDB / ID: 2kt5 | ||||||
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Title | RRM domain of mRNA export adaptor REF2-I bound to HSV-1 ICP27 peptide | ||||||
Components |
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Keywords | RNA Binding Protein / Viral Protein / REF ICP27 HSV-1 / Chaperone / mRNA processing / mRNA splicing / mRNA transport / Nucleus / RNA-binding / Spliceosome / Transport / RNA Binding Protein - Viral Protein complex | ||||||
Function / homology | Function and homology information viral mRNA export from host cell nucleus / transcription export complex / C5-methylcytidine-containing RNA reader activity / regulation of DNA recombination / RNA export from nucleus / positive regulation of DNA-templated transcription, elongation / replication fork processing / mRNA transport / mRNA export from nucleus / catalytic step 2 spliceosome ...viral mRNA export from host cell nucleus / transcription export complex / C5-methylcytidine-containing RNA reader activity / regulation of DNA recombination / RNA export from nucleus / positive regulation of DNA-templated transcription, elongation / replication fork processing / mRNA transport / mRNA export from nucleus / catalytic step 2 spliceosome / RNA splicing / mRNA processing / single-stranded DNA binding / mRNA binding / regulation of DNA-templated transcription / RNA binding / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) Human herpesvirus 1 (Herpes simplex virus type 1) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Tunnicliffe, N.B. / Golovanov, A.P. / Wilson, S.A. / Hautbergue, G.M. | ||||||
Citation | Journal: Plos Pathog. / Year: 2011 Title: Structural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57. Authors: Tunnicliffe, R.B. / Hautbergue, G.M. / Kalra, P. / Jackson, B.R. / Whitehouse, A. / Wilson, S.A. / Golovanov, A.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2kt5.cif.gz | 968.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2kt5.ent.gz | 842.8 KB | Display | PDB format |
PDBx/mmJSON format | 2kt5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kt/2kt5 ftp://data.pdbj.org/pub/pdb/validation_reports/kt/2kt5 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 13596.133 Da / Num. of mol.: 1 / Fragment: RRM domain, residues 53-155 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Refbp2, Ref2 / Plasmid: pET24b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) RP / References: UniProt: Q9JJW6 |
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#2: Protein/peptide | Mass: 4268.931 Da / Num. of mol.: 1 / Fragment: REF interaction fragment, residues 103-138 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human herpesvirus 1 (Herpes simplex virus type 1) Plasmid: pGEX-6P-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) RP / References: UniProt: Q9J0X9 |
-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: 50 / pH: 6.2 / Pressure: AMBIENT bar / Temperature: 303 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / 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 |