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Yorodumi- PDB-1jgn: Solution structure of the C-terminal PABC domain of human poly(A)... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jgn | ||||||
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Title | Solution structure of the C-terminal PABC domain of human poly(A)-binding protein in complex with the peptide from Paip2 | ||||||
Components |
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Keywords | RNA BINDING PROTEIN / all-helical domain / protein-peptide complex | ||||||
Function / homology | Function and homology information negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / mCRD-mediated mRNA stability complex / translation activator activity / negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CRD-mediated mRNA stabilization / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / Deadenylation of mRNA / positive regulation of cytoplasmic translation / M-decay: degradation of maternal mRNAs by maternally stored factors / poly(A) binding ...negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / mCRD-mediated mRNA stability complex / translation activator activity / negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / CRD-mediated mRNA stabilization / Z-decay: degradation of maternal mRNAs by zygotically expressed factors / Deadenylation of mRNA / positive regulation of cytoplasmic translation / M-decay: degradation of maternal mRNAs by maternally stored factors / poly(A) binding / regulatory ncRNA-mediated gene silencing / mRNA stabilization / poly(U) RNA binding / regulation of long-term synaptic potentiation / positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / Translation initiation complex formation / cell leading edge / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / L13a-mediated translational silencing of Ceruloplasmin expression / positive regulation of viral genome replication / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / translation repressor activity / negative regulation of translational initiation / catalytic step 2 spliceosome / mRNA regulatory element binding translation repressor activity / AUF1 (hnRNP D0) binds and destabilizes mRNA / mRNA 3'-UTR binding / memory / Regulation of expression of SLITs and ROBOs / mRNA splicing, via spliceosome / cytoplasmic stress granule / cytoplasmic ribonucleoprotein granule / lamellipodium / spermatogenesis / negative regulation of translation / translation / ribonucleoprotein complex / focal adhesion / mRNA binding / RNA binding / extracellular exosome / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Kozlov, G. / Siddiqui, N. / Coillet-Matillon, S. / Ekiel, I. / Gehring, K. | ||||||
Citation | Journal: EMBO J. / Year: 2004 Title: Structural basis of ligand recognition by PABC, a highly specific peptide-binding domain found in poly(A)-binding protein and a HECT ubiquitin ligase Authors: Kozlov, G. / De Crescenzo, G. / Lim, N.S. / Siddiqui, N. / Fantus, D. / Kahvejian, A. / Trempe, J.F. / Elias, D. / Ekiel, I. / Sonenberg, N. / O'Connor-McCourt, M. / Gehring, K. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 2001 Title: Structure and function of the C-terminal PABC domain of human poly(A)-binding protein Authors: Kozlov, G. / Trempe, J.F. / Khaleghpour, K. / Kahvejian, A. / Ekiel, I. / Gehring, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jgn.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1jgn.ent.gz | 880.6 KB | Display | PDB format |
PDBx/mmJSON format | 1jgn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jgn_validation.pdf.gz | 356.3 KB | Display | wwPDB validaton report |
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Full document | 1jgn_full_validation.pdf.gz | 808.7 KB | Display | |
Data in XML | 1jgn_validation.xml.gz | 88.6 KB | Display | |
Data in CIF | 1jgn_validation.cif.gz | 113 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jg/1jgn ftp://data.pdbj.org/pub/pdb/validation_reports/jg/1jgn | HTTPS FTP |
-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 | Mass: 10347.936 Da / Num. of mol.: 1 / Fragment: C-terminal domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PABPC1 / Plasmid: pGEX-6P-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 GOLD / References: UniProt: P11940 |
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#2: Protein/peptide | Mass: 2390.755 Da / Num. of mol.: 1 / Fragment: C-terminal 22 residues Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGEX-6P-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 GOLD / References: UniProt: Q9BPZ3 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using standard triple-resonance and homonuclear techniques |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 0.1M NaCl / pH: 6.3 / Pressure: ambient / Temperature: 303 K | |||||||||||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-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: simulated annealing / Software ordinal: 1 Details: The structures are based on 2058 non-redundant NOE-derived distance constraints, 106 dihedral angle restraints, and 35 hydrogen bonds. | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 30 |