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Yorodumi- PDB-1cvj: X-RAY CRYSTAL STRUCTURE OF THE POLY(A)-BINDING PROTEIN IN COMPLEX... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1cvj | |||||||||
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Title | X-RAY CRYSTAL STRUCTURE OF THE POLY(A)-BINDING PROTEIN IN COMPLEX WITH POLYADENYLATE RNA | |||||||||
Components |
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Keywords | GENE REGULATION/RNA / RRM / PROTEIN-RNA COMPLEX / GENE REGULATION-RNA COMPLEX | |||||||||
Function / homology | Function and homology information mCRD-mediated mRNA stability complex / negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / 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 ...mCRD-mediated mRNA stability complex / negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / 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 / 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) / catalytic step 2 spliceosome / mRNA 3'-UTR binding / AUF1 (hnRNP D0) binds and destabilizes mRNA / mRNA splicing, via spliceosome / Regulation of expression of SLITs and ROBOs / cytoplasmic ribonucleoprotein granule / cytoplasmic stress granule / lamellipodium / ribonucleoprotein complex / focal adhesion / mRNA binding / RNA binding / extracellular exosome / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.6 Å | |||||||||
Authors | Deo, R.C. / Bonanno, J.B. / Sonenberg, N. / Burley, S.K. | |||||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1999 Title: Recognition of polyadenylate RNA by the poly(A)-binding protein. Authors: Deo, R.C. / Bonanno, J.B. / Sonenberg, N. / Burley, S.K. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cvj.cif.gz | 288.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cvj.ent.gz | 231.3 KB | Display | PDB format |
PDBx/mmJSON format | 1cvj.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1cvj_validation.pdf.gz | 862.1 KB | Display | wwPDB validaton report |
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Full document | 1cvj_full_validation.pdf.gz | 934.7 KB | Display | |
Data in XML | 1cvj_validation.xml.gz | 36.4 KB | Display | |
Data in CIF | 1cvj_validation.cif.gz | 55.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cv/1cvj ftp://data.pdbj.org/pub/pdb/validation_reports/cv/1cvj | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
-Components
#1: RNA chain | Mass: 3576.306 Da / Num. of mol.: 8 / Source method: obtained synthetically #2: Protein | Mass: 21463.604 Da / Num. of mol.: 8 / Fragment: RESIDUES 1-190 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PGEX6P1 / Production host: Escherichia coli (E. coli) / References: UniProt: P11940 #3: Chemical | ChemComp-AMP / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 52.03 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 296.7 K / Method: vapor diffusion, hanging drop / pH: 8 Details: AMMONIUM SULFATE, TCEP, TRIS-HCL, POTASSIUM CHLORIDE, GLYCEROL, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 296.7K | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions |
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Crystal grow | *PLUS Temperature: 24 ℃ / Details: a 1 : 1.2 protein : RNA ratio | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength |
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Reflection | Resolution: 2.6→20 Å / Num. all: 61125 / Num. obs: 61125 / % possible obs: 99.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Biso Wilson estimate: 60 Å2 / Rmerge(I) obs: 0.053 / Net I/σ(I): 19 | ||||||||||||||||||||
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 3 % / Rmerge(I) obs: 0.294 / % possible all: 99.7 | ||||||||||||||||||||
Reflection | *PLUS |
-Processing
Software |
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Refinement | Resolution: 2.6→20 Å / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 2.6→20 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 20 Å / σ(F): 2 / % reflection Rfree: 10 % / Rfactor obs: 0.23 / Rfactor Rwork: 0.23 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |