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Yorodumi- PDB-1v5m: Solution Structure of the Pleckstrin Homology Domain of Mouse APS -
+Open data
-Basic information
Entry | Database: PDB / ID: 1v5m | ||||||
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Title | Solution Structure of the Pleckstrin Homology Domain of Mouse APS | ||||||
Components | SH2 and PH domain-containing adapter protein APS | ||||||
Keywords | PROTEIN BINDING / adaptor protein / Pleckstrin Homology domain / cellular signaling / structural genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information antigen receptor-mediated signaling pathway / Regulation of KIT signaling / regulation of Ras protein signal transduction / Factors involved in megakaryocyte development and platelet production / B-1 B cell homeostasis / regulation of metabolic process / negative regulation of glucose import / transmembrane receptor protein tyrosine kinase adaptor activity / regulation of immune response / signaling adaptor activity ...antigen receptor-mediated signaling pathway / Regulation of KIT signaling / regulation of Ras protein signal transduction / Factors involved in megakaryocyte development and platelet production / B-1 B cell homeostasis / regulation of metabolic process / negative regulation of glucose import / transmembrane receptor protein tyrosine kinase adaptor activity / regulation of immune response / signaling adaptor activity / brown fat cell differentiation / stress fiber / ruffle / SH2 domain binding / actin filament / B cell receptor signaling pathway / cytokine-mediated signaling pathway / insulin receptor signaling pathway / glucose homeostasis / nervous system development / actin cytoskeleton organization / intracellular signal transduction / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Li, H. / Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution Structure of the Pleckstrin Homology Domain of Mouse APS Authors: Li, H. / Tochio, N. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1v5m.cif.gz | 801.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1v5m.ent.gz | 673.3 KB | Display | PDB format |
PDBx/mmJSON format | 1v5m.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v5/1v5m ftp://data.pdbj.org/pub/pdb/validation_reports/v5/1v5m | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14689.724 Da / Num. of mol.: 1 / Fragment: Pleckstrin Homology Domain / Mutation: T8N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Description: Cell-free protein synthesis / Gene: RIKEN cDNA 5730427K19 / Plasmid: P030212-26 / References: UniProt: Q9JID9 |
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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: 1.23mM Pleckstrin Homology domain U-13C, 15N; 20mM d-Tris-HCl(7.5); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
-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 least restraint violations, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |