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- PDB-8xrp: The Cryo-EM structure of IL-12, receptor subunit beta-1 and recep... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8xrp | ||||||
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Title | The Cryo-EM structure of IL-12, receptor subunit beta-1 and receptor subunit beta-2 complex | ||||||
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![]() | CYTOKINE / IL-12 / IL-12RB1 / IL-12RB2 / receptor complex | ||||||
Function / homology | ![]() interleukin-27 binding / interleukin-12 beta subunit binding / late endosome lumen / interleukin-23-mediated signaling pathway / regulation of tyrosine phosphorylation of STAT protein / interleukin-12 alpha subunit binding / interleukin-12 complex / interleukin-23 complex / natural killer cell activation involved in immune response / positive regulation of dendritic cell chemotaxis ...interleukin-27 binding / interleukin-12 beta subunit binding / late endosome lumen / interleukin-23-mediated signaling pathway / regulation of tyrosine phosphorylation of STAT protein / interleukin-12 alpha subunit binding / interleukin-12 complex / interleukin-23 complex / natural killer cell activation involved in immune response / positive regulation of dendritic cell chemotaxis / positive regulation of natural killer cell activation / positive regulation of lymphocyte proliferation / positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of vascular endothelial growth factor signaling pathway / negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / positive regulation of tissue remodeling / positive regulation of activation of Janus kinase activity / sexual reproduction / positive regulation of T-helper 1 type immune response / positive regulation of NK T cell activation / positive regulation of smooth muscle cell apoptotic process / positive regulation of natural killer cell mediated cytotoxicity / positive regulation of mononuclear cell proliferation / interleukin-12 receptor binding / positive regulation of memory T cell differentiation / interleukin-12 receptor complex / natural killer cell activation / T-helper cell differentiation / interleukin-23 receptor complex / positive regulation of osteoclast differentiation / Interleukin-23 signaling / negative regulation of interleukin-17 production / positive regulation of T-helper 17 type immune response / positive regulation of NK T cell proliferation / interleukin-12-mediated signaling pathway / Interleukin-12 signaling / Interleukin-35 Signalling / response to UV-B / positive regulation of natural killer cell proliferation / positive regulation of granulocyte macrophage colony-stimulating factor production / cytokine receptor activity / T-helper 1 type immune response / negative regulation of interleukin-10 production / cytokine binding / positive regulation of activated T cell proliferation / defense response to protozoan / positive regulation of interleukin-17 production / Interleukin-10 signaling / positive regulation of interleukin-10 production / positive regulation of cell adhesion / negative regulation of protein secretion / coreceptor activity / positive regulation of T-helper 17 cell lineage commitment / T cell proliferation / extrinsic apoptotic signaling pathway / positive regulation of T cell proliferation / positive regulation of tyrosine phosphorylation of STAT protein / negative regulation of inflammatory response to antigenic stimulus / positive regulation of defense response to virus by host / regulation of cytokine production / positive regulation of interleukin-12 production / cytokine activity / negative regulation of smooth muscle cell proliferation / growth factor activity / response to virus / cellular response to virus / cytokine-mediated signaling pathway / cellular response to type II interferon / positive regulation of inflammatory response / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of T cell mediated cytotoxicity / positive regulation of tumor necrosis factor production / positive regulation of type II interferon production / cell migration / cellular response to lipopolysaccharide / Interleukin-4 and Interleukin-13 signaling / defense response to Gram-negative bacterium / defense response to virus / response to lipopolysaccharide / cell surface receptor signaling pathway / receptor complex / defense response to Gram-positive bacterium / immune response / protein heterodimerization activity / endoplasmic reticulum lumen / external side of plasma membrane / positive regulation of cell population proliferation / protein-containing complex binding / protein kinase binding / signal transduction / extracellular space / extracellular region / identical protein binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.75 Å | ||||||
![]() | Chen, H.Q. / Wang, X.Q. / Ge, X.F. / Zeng, J.W. / Wang, J.W. | ||||||
Funding support | ![]()
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![]() | ![]() Title: The Cryo-EM structure of IL-12/IL-12RB1-D1/IL-12RB2-D1-D3 complex Authors: Chen, H.Q. / Wang, X.Q. / Ge, X.F. / Zeng, J.W. / Wang, J.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 | ![]() | 641.6 KB | Display | ![]() |
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PDB format | ![]() | 521.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.9 MB | Display | ![]() |
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Full document | ![]() | 1.9 MB | Display | |
Data in XML | ![]() | 106.7 KB | Display | |
Data in CIF | ![]() | 159 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 38609MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
-Interleukin-12 subunit ... , 2 types, 8 molecules AEIMBFJN
#1: Protein | Mass: 23781.508 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: Interleukin-12 subunit alpha / Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 34811.023 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: Interleukin-12 subunit beta / Source: (gene. exp.) ![]() ![]() |
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-Interleukin-12 receptor subunit beta- ... , 2 types, 8 molecules CGKODHLP
#3: Protein | Mass: 34627.477 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: Interleukin-12 receptor subunit beta-2 / Source: (gene. exp.) ![]() ![]() #4: Protein | Mass: 24736.449 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: Interleukin-12 receptor subunit beta-1 / Source: (gene. exp.) ![]() ![]() |
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-Sugars , 2 types, 16 molecules ![](data/chem/img/NAG.gif)
#5: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #6: Sugar | ChemComp-NAG / |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
Component | Name: The Cryo-EM structure of IL-12, receptor subunit beta-1 and receptor subunit beta-2 complex Type: COMPLEX / Entity ID: #1-#4 / Source: RECOMBINANT | |||||||||||||||
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Molecular weight | Value: 0.485 MDa / Experimental value: NO | |||||||||||||||
Source (natural) | Organism: ![]() | |||||||||||||||
Source (recombinant) | Organism: ![]() | |||||||||||||||
Buffer solution | pH: 8 / Details: 25mM Tris-HCl pH 8.0,150mM NaCl | |||||||||||||||
Buffer component |
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Specimen | Conc.: 1.34 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||
Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil | |||||||||||||||
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 500 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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Particle selection | Num. of particles selected: 4547423 |
3D reconstruction | Resolution: 3.75 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 423691 / Symmetry type: POINT |