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Yorodumi- PDB-2na8: Transmembrane Structure of the Cytokine Receptor Common Subunit beta -
+Open data
-Basic information
Entry | Database: PDB / ID: 2na8 | ||||||
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Title | Transmembrane Structure of the Cytokine Receptor Common Subunit beta | ||||||
Components | Cytokine receptor common subunit beta | ||||||
Keywords | MEMBRANE PROTEIN / transmembrane helix | ||||||
Function / homology | Function and homology information Defective CSF2RB causes SMDP5 / Defective CSF2RA causes SMDP4 / respiratory gaseous exchange by respiratory system / Surfactant metabolism / granulocyte macrophage colony-stimulating factor receptor complex / granulocyte-macrophage colony-stimulating factor signaling pathway / interleukin-5-mediated signaling pathway / positive regulation of leukocyte proliferation / interleukin-3-mediated signaling pathway / cellular response to interleukin-3 ...Defective CSF2RB causes SMDP5 / Defective CSF2RA causes SMDP4 / respiratory gaseous exchange by respiratory system / Surfactant metabolism / granulocyte macrophage colony-stimulating factor receptor complex / granulocyte-macrophage colony-stimulating factor signaling pathway / interleukin-5-mediated signaling pathway / positive regulation of leukocyte proliferation / interleukin-3-mediated signaling pathway / cellular response to interleukin-3 / cytokine receptor activity / cell surface receptor signaling pathway via JAK-STAT / Interleukin-3, Interleukin-5 and GM-CSF signaling / immunoglobulin mediated immune response / Interleukin receptor SHC signaling / coreceptor activity / cytokine-mediated signaling pathway / signaling receptor activity / RAF/MAP kinase cascade / response to lipopolysaccharide / external side of plasma membrane / signal transduction / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | minimized average structure, model21 | ||||||
Model type details | minimized average | ||||||
Authors | Schmidt, T. / Ye, F. / Situ, A.J. / An, W. / Ginsberg, M.H. / Ulmer, T.S. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2016 Title: A Conserved Ectodomain-Transmembrane Domain Linker Motif Tunes the Allosteric Regulation of Cell Surface Receptors. Authors: Schmidt, T. / Ye, F. / Situ, A.J. / An, W. / Ginsberg, M.H. / Ulmer, T.S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2na8.cif.gz | 315.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2na8.ent.gz | 264.5 KB | Display | PDB format |
PDBx/mmJSON format | 2na8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/na/2na8 ftp://data.pdbj.org/pub/pdb/validation_reports/na/2na8 | 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: 5146.282 Da / Num. of mol.: 1 / Fragment: Helical transmembrane residues 432-473 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CSF2RB, IL3RB, IL5RB / Production host: Escherichia coli (E. coli) / References: UniProt: P32927 |
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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: 0.5 mM [U-99% 13C; U-99% 15N; 80% 2H] protein, 93% H2O/7% D2O Solvent system: 93% H2O/7% D2O |
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Sample | Conc.: 0.5 mM / Component: entity-1 / Isotopic labeling: [U-99% 13C; U-99% 15N; 80% 2H] |
Sample conditions | Ionic strength: 0.05 / pH: 7.4 / Pressure: ambient / Temperature: 313 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||
NMR representative | Selection criteria: minimized average structure | |||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 21 / Conformers submitted total number: 21 |