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Yorodumi- PDB-1txp: Heterogeneous Nuclear Ribonucleoprotein (hnRNP) C Oligomerization... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1txp | ||||||
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Title | Heterogeneous Nuclear Ribonucleoprotein (hnRNP) C Oligomerization Domain Tetramer | ||||||
Components | Heterogeneous Nuclear Ribonucleoprotein C protein | ||||||
Keywords | SIGNALING PROTEIN / Antiparallel Four Helix Coiled Coil Tetramer hnRNPC | ||||||
Function / homology | Function and homology information chromatin remodeling => GO:0006338 / RNA metabolic process / chromatin => GO:0000785 / N6-methyladenosine-containing RNA reader activity / telomerase holoenzyme complex / SUMOylation of RNA binding proteins / telomerase RNA binding / poly(U) RNA binding / RHOBTB1 GTPase cycle / 3'-UTR-mediated mRNA stabilization ...chromatin remodeling => GO:0006338 / RNA metabolic process / chromatin => GO:0000785 / N6-methyladenosine-containing RNA reader activity / telomerase holoenzyme complex / SUMOylation of RNA binding proteins / telomerase RNA binding / poly(U) RNA binding / RHOBTB1 GTPase cycle / 3'-UTR-mediated mRNA stabilization / Processing of Capped Intron-Containing Pre-mRNA / negative regulation of telomere maintenance via telomerase / nucleosomal DNA binding / RHOBTB2 GTPase cycle / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / RNA splicing / mRNA 3'-UTR binding / spliceosomal complex / mRNA splicing, via spliceosome / osteoblast differentiation / actin cytoskeleton / chromatin remodeling / chromatin / protein-containing complex / RNA binding / extracellular exosome / extracellular region / nucleoplasm / membrane / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Whitson, S.R. / Lestourgeon, W.M. / Krezel, A.M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2005 Title: Solution Structure of the Symmetric Coiled Coil Tetramer Formed by the Oligomerization Domain of hnRNP C: Implications for Biological Function. Authors: Whitson, S.R. / Lestourgeon, W.M. / Krezel, A.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1txp.cif.gz | 754.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1txp.ent.gz | 645.9 KB | Display | PDB format |
PDBx/mmJSON format | 1txp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tx/1txp ftp://data.pdbj.org/pub/pdb/validation_reports/tx/1txp | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3315.893 Da / Num. of mol.: 4 / Fragment: Oligomerization Domain / Mutation: L180I Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HnRNP C1 / Plasmid: pET32(LIC) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q86U45, UniProt: P07910*PLUS |
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-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 conditions | Ionic strength: 0 mM NaCl / pH: 6.0 / Pressure: ambient / Temperature: 300 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: Structures are based on 1628 total constraints, including 1308 NOE-derived distance constraints, 244 dihedral angle restraints and 76 hydrogen bond distance restraints. | ||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 |