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Yorodumi- PDB-2l5j: structure of the spliceosomal phosphopeptide P140 (phosphorylated... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2l5j | ||||||
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Title | structure of the spliceosomal phosphopeptide P140 (phosphorylated form) | ||||||
Components | U1 small nuclear ribonucleoprotein 70 kDa | ||||||
Keywords | SPLICING / phosphorylation / HSC70 / Lupus | ||||||
Function / homology | Function and homology information negative regulation of protein refolding / regulation of ATP-dependent activity / negative regulation of chaperone-mediated autophagy / positive regulation of mRNA splicing, via spliceosome / U1 snRNP / U2-type prespliceosome / precatalytic spliceosome / regulation of RNA splicing / U1 snRNA binding / mRNA Splicing - Major Pathway ...negative regulation of protein refolding / regulation of ATP-dependent activity / negative regulation of chaperone-mediated autophagy / positive regulation of mRNA splicing, via spliceosome / U1 snRNP / U2-type prespliceosome / precatalytic spliceosome / regulation of RNA splicing / U1 snRNA binding / mRNA Splicing - Major Pathway / spliceosomal complex / mRNA splicing, via spliceosome / nuclear speck / mRNA binding / RNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | fewest violations, model 1 | ||||||
Authors | Quinternet, M. / Page, N. / Schall, N. / Strub, J. / Chaloin, O. / Decossas, M. / Cung, M. / van Dorsselaer, A. / Briand, J. / Muller, S. | ||||||
Citation | Journal: Plos One / Year: 2009 Title: The spliceosomal phosphopeptide P140 controls the lupus disease by interacting with the HSC70 protein and via a mechanism mediated by gammadelta T cells. Authors: Page, N. / Schall, N. / Strub, J.M. / Quinternet, M. / Chaloin, O. / Decossas, M. / Cung, M.T. / Van Dorsselaer, A. / Briand, J.P. / Muller, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l5j.cif.gz | 56.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l5j.ent.gz | 44.9 KB | Display | PDB format |
PDBx/mmJSON format | 2l5j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l5/2l5j ftp://data.pdbj.org/pub/pdb/validation_reports/l5/2l5j | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 2644.985 Da / Num. of mol.: 1 / Fragment: UNP residues 131-151 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P08621 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 2 mM entity-1, 95% H2O/5% D2O / Solvent system: 95% H2O/5% D2O |
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Sample | Conc.: 2 mM / Component: entity-1 |
Sample conditions | Ionic strength: 0 / pH: 4 / Pressure: ambient / Temperature: 278 K |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: fewest violations | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 8 |