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Open data
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Basic information
Entry | Database: PDB / ID: 4nkq | |||||||||
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Title | Structure of a Cytokine Receptor Complex | |||||||||
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![]() | CYTOKINE/CYTOKINE RECEPTOR / GM-CSF / receptor complex / dodecamer / Disease mutation / Glycoprotein / Membrane / Phosphoprotein / Transmembrane / Cytokine / Growth factor / Secreted / CYTOKINE-CYTOKINE RECEPTOR complex | |||||||||
Function / homology | ![]() granulocyte macrophage colony-stimulating factor receptor binding / histamine secretion / neutrophil differentiation / response to silicon dioxide / Defective CSF2RB causes SMDP5 / Defective CSF2RA causes SMDP4 / epithelial fluid transport / positive regulation of interleukin-23 production / regulation of circadian sleep/wake cycle, sleep / dendritic cell differentiation ...granulocyte macrophage colony-stimulating factor receptor binding / histamine secretion / neutrophil differentiation / response to silicon dioxide / Defective CSF2RB causes SMDP5 / Defective CSF2RA causes SMDP4 / epithelial fluid transport / positive regulation of interleukin-23 production / regulation of circadian sleep/wake cycle, sleep / dendritic cell differentiation / response to fluid shear stress / positive regulation of macrophage derived foam cell differentiation / respiratory gaseous exchange by respiratory system / myeloid dendritic cell differentiation / Surfactant metabolism / granulocyte macrophage colony-stimulating factor receptor complex / granulocyte-macrophage colony-stimulating factor signaling pathway / interleukin-5-mediated signaling pathway / myeloid cell differentiation / positive regulation of leukocyte proliferation / cellular response to granulocyte macrophage colony-stimulating factor stimulus / cellular response to interleukin-3 / interleukin-3-mediated signaling pathway / RUNX1 regulates transcription of genes involved in differentiation of myeloid cells / positive regulation of podosome assembly / cytokine receptor activity / cytokine binding / Interleukin-10 signaling / cell surface receptor signaling pathway via JAK-STAT / monocyte differentiation / macrophage differentiation / Interleukin-3, Interleukin-5 and GM-CSF signaling / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / immunoglobulin mediated immune response / embryonic placenta development / Interleukin receptor SHC signaling / coreceptor activity / positive regulation of tyrosine phosphorylation of STAT protein / cytokine activity / growth factor activity / cytokine-mediated signaling pathway / signaling receptor activity / RAF/MAP kinase cascade / cellular response to lipopolysaccharide / cell population proliferation / response to lipopolysaccharide / receptor complex / positive regulation of cell migration / immune response / external side of plasma membrane / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / positive regulation of gene expression / signal transduction / extracellular space / extracellular region / plasma membrane Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Parker, M.W. / Broughton, S.E. | |||||||||
![]() | ![]() Title: Conformational Changes in the GM-CSF Receptor Suggest a Molecular Mechanism for Affinity Conversion and Receptor Signaling. Authors: Broughton, S.E. / Hercus, T.R. / Nero, T.L. / Dottore, M. / McClure, B.J. / Dhagat, U. / Taing, H. / Gorman, M.A. / King-Scott, J. / Lopez, A.F. / Parker, M.W. #1: Journal: Cell(Cambridge,Mass.) / Year: 2008 Title: The structure of the GM-CSF receptor complex reveals a distinct mode of cytokine receptor activation. Authors: Hansen, G. / Hercus, T.R. / McClure, B.J. / Stomski, F.C. / Dottore, M. / Powell, J. / Ramshaw, H. / Woodcock, J.M. / Xu, Y. / Guthridge, M. / McKinstry, W.J. / Lopez, A.F. / Parker, M.W. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 307.9 KB | Display | ![]() |
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PDB format | ![]() | 255.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 480.8 KB | Display | ![]() |
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Full document | ![]() | 513.8 KB | Display | |
Data in XML | ![]() | 30.6 KB | Display | |
Data in CIF | ![]() | 40.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 47258.754 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Protein | Mass: 14492.495 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
#3: Protein | Mass: 34850.496 Da / Num. of mol.: 1 / Mutation: N346Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
#4: Sugar | ChemComp-NAG / Sequence details | FOR CHAIN B THE IDENTITY OF THE RESIDUES 23-25, 44-50, 68-74 IS UNKNOWN. THESE RESIDUES ARE LISTED ...FOR CHAIN B THE IDENTITY OF THE RESIDUES 23-25, 44-50, 68-74 IS UNKNOWN. THESE RESIDUES ARE LISTED AS UNK (UNKNOWN RESIDUE). THE COMPLETE CRYSTALLIZ | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.42 Å3/Da / Density % sol: 72.19 % |
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Crystal grow | Temperature: 293 K / pH: 7 Details: 100mM HEPES buffer (pH 7.0), 6%(v/v) PEG3350, 0.2M proline, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 30, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 3.3→36.08 Å / Num. obs: 26765 / % possible obs: 99.5 % / Rmerge(I) obs: 0.077 |
Reflection shell | Resolution: 3.2→3.48 Å / % possible all: 99.5 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.301→36.082 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 51.7821 Å / Origin y: -45.5912 Å / Origin z: -32.3813 Å
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Refinement TLS group | Selection details: all |