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- PDB-1rqq: Crystal Structure of the Insulin Receptor Kinase in Complex with ... -
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Basic information
Entry | Database: PDB / ID: 1rqq | ||||||
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Title | Crystal Structure of the Insulin Receptor Kinase in Complex with the SH2 Domain of APS | ||||||
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![]() | TRANSFERASE/SIGNALING PROTEIN / Protein tyrosine kinase / adaptor protein / SH2 domain / TRANSFERASE-SIGNALING PROTEIN COMPLEX | ||||||
Function / homology | ![]() Regulation of KIT signaling / Factors involved in megakaryocyte development and platelet production / antigen receptor-mediated signaling pathway / regulation of Ras protein signal transduction / regulation of female gonad development / positive regulation of meiotic cell cycle / B-1 B cell homeostasis / positive regulation of developmental growth / insulin-like growth factor II binding / male sex determination ...Regulation of KIT signaling / Factors involved in megakaryocyte development and platelet production / antigen receptor-mediated signaling pathway / regulation of Ras protein signal transduction / regulation of female gonad development / positive regulation of meiotic cell cycle / B-1 B cell homeostasis / positive regulation of developmental growth / insulin-like growth factor II binding / male sex determination / exocrine pancreas development / insulin receptor complex / regulation of metabolic process / insulin-like growth factor I binding / insulin receptor activity / transmembrane receptor protein tyrosine kinase adaptor activity / positive regulation of protein-containing complex disassembly / cargo receptor activity / dendritic spine maintenance / insulin binding / PTB domain binding / adrenal gland development / neuronal cell body membrane / Signaling by Insulin receptor / IRS activation / activation of protein kinase activity / amyloid-beta clearance / positive regulation of respiratory burst / positive regulation of receptor internalization / regulation of embryonic development / transport across blood-brain barrier / insulin receptor substrate binding / positive regulation of glycogen biosynthetic process / regulation of immune response / epidermis development / Signal attenuation / phosphatidylinositol 3-kinase binding / signaling adaptor activity / brown fat cell differentiation / heart morphogenesis / stress fiber / dendrite membrane / ruffle / Insulin receptor recycling / neuron projection maintenance / positive regulation of glycolytic process / activation of protein kinase B activity / SH2 domain binding / positive regulation of mitotic nuclear division / Insulin receptor signalling cascade / receptor-mediated endocytosis / learning / caveola / actin filament / positive regulation of glucose import / B cell receptor signaling pathway / insulin-like growth factor receptor binding / positive regulation of MAP kinase activity / receptor internalization / receptor protein-tyrosine kinase / memory / cellular response to growth factor stimulus / cytokine-mediated signaling pathway / peptidyl-tyrosine phosphorylation / cellular response to insulin stimulus / male gonad development / positive regulation of nitric oxide biosynthetic process / late endosome / insulin receptor signaling pathway / glucose homeostasis / nervous system development / amyloid-beta binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / actin cytoskeleton organization / protein tyrosine kinase activity / positive regulation of MAPK cascade / protein autophosphorylation / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / lysosome / receptor complex / endosome membrane / intracellular signal transduction / positive regulation of cell migration / symbiont entry into host cell / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / protein domain specific binding / external side of plasma membrane / axon / protein phosphorylation / positive regulation of cell population proliferation / protein-containing complex binding / regulation of DNA-templated transcription / GTP binding / positive regulation of DNA-templated transcription / extracellular exosome / ATP binding / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Hu, J. / Liu, J. / Ghirlando, R. / Saltiel, A.R. / Hubbard, S.R. | ||||||
![]() | ![]() Title: Structural basis for recruitment of the adaptor protein APS to the activated insulin receptor. Authors: Hu, J. / Liu, J. / Ghirlando, R. / Saltiel, A.R. / Hubbard, S.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 172.3 KB | Display | ![]() |
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PDB format | ![]() | 133.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 32.1 KB | Display | |
Data in CIF | ![]() | 43.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1rpySC ![]() 1gagS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 2 types, 4 molecules ABCD
#1: Protein | Mass: 35033.660 Da / Num. of mol.: 2 / Fragment: Kinase domain / Mutation: C980S, K1251N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 12891.678 Da / Num. of mol.: 2 / Fragment: SH2 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Protein/peptide , 1 types, 2 molecules EF
#3: Protein/peptide | Mass: 1939.280 Da / Num. of mol.: 2 / Source method: obtained synthetically |
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-Non-polymers , 3 types, 83 molecules ![](data/chem/img/MN.gif)
![](data/chem/img/112.gif)
![](data/chem/img/HOH.gif)
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#4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 56 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8 / Details: pH 8.0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: CCD / Date: Nov 3, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→50 Å / Num. obs: 32437 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 4.8 % / Rsym value: 0.039 / Net I/σ(I): 22.4 |
Reflection shell | Resolution: 2.6→2.69 Å / Rsym value: 0.164 / % possible all: 99.4 |
Reflection | *PLUS Lowest resolution: 30 Å / Num. measured all: 156301 / Rmerge(I) obs: 0.039 |
Reflection shell | *PLUS % possible obs: 99.4 % / Rmerge(I) obs: 0.164 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRIES 1GAG, 1RPY Resolution: 2.6→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Solvent computation | Solvent model: CNS / Bsol: 31.06 Å2 / ksol: 0.32 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 49.9 Å2
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Refinement step | Cycle: LAST / Resolution: 2.6→30 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 30 Å / Num. reflection obs: 31461 / % reflection Rfree: 5 % / Rfactor Rfree: 0.279 / Rfactor Rwork: 0.233 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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