+Open data
-Basic information
Entry | Database: PDB / ID: 4im8 | ||||||
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Title | low resolution crystal structure of mouse RAGE | ||||||
Components | Advanced glycation end-products receptor | ||||||
Keywords | SIGNALING PROTEIN / heparan sulfate | ||||||
Function / homology | Function and homology information positive regulation of signaling / high mobility group box 1 binding / advanced glycation end-product binding / negative regulation of advanced glycation end-product receptor activity / positive regulation of advanced glycation end-product receptor activity / positive regulation of chemokine production => GO:0032722 / positive regulation of tumor necrosis factor production => GO:0032760 / Advanced glycosylation endproduct receptor signaling / regulation of DNA binding / : ...positive regulation of signaling / high mobility group box 1 binding / advanced glycation end-product binding / negative regulation of advanced glycation end-product receptor activity / positive regulation of advanced glycation end-product receptor activity / positive regulation of chemokine production => GO:0032722 / positive regulation of tumor necrosis factor production => GO:0032760 / Advanced glycosylation endproduct receptor signaling / regulation of DNA binding / : / negative regulation of signaling / regulation of CD4-positive, alpha-beta T cell activation / : / negative regulation of blood circulation / regulation of T cell mediated cytotoxicity / positive regulation of potassium ion transmembrane transporter activity / positive regulation of endothelin production / glucose mediated signaling pathway / negative regulation of long-term synaptic depression / positive regulation of monocyte extravasation / TRAF6 mediated NF-kB activation / positive regulation of type B pancreatic cell apoptotic process / positive regulation of dendritic cell differentiation / positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process / regulation of p38MAPK cascade / TAK1-dependent IKK and NF-kappa-B activation / negative regulation of collagen biosynthetic process / positive regulation of phagocytosis, engulfment / astrocyte development / induction of positive chemotaxis / transcytosis / negative regulation of cell adhesion / positive regulation of endothelial cell apoptotic process / protein localization to membrane / positive regulation of monocyte chemotactic protein-1 production / negative regulation of endothelial cell migration / positive regulation of fibroblast migration / negative regulation of connective tissue replacement involved in inflammatory response wound healing / S100 protein binding / regulation of long-term synaptic potentiation / regulation of spontaneous synaptic transmission / positive regulation of heterotypic cell-cell adhesion / positive regulation of p38MAPK cascade / negative regulation of interleukin-10 production / negative regulation of endothelial cell proliferation / positive regulation of activated T cell proliferation / positive regulation of smooth muscle cell migration / negative regulation of long-term synaptic potentiation / cell surface receptor signaling pathway via JAK-STAT / response to amyloid-beta / transport across blood-brain barrier / positive regulation of epithelial to mesenchymal transition / calcium ion homeostasis / positive regulation of autophagy / positive regulation of JUN kinase activity / positive regulation of interleukin-12 production / basal plasma membrane / negative regulation of cell migration / negative regulation of protein phosphorylation / positive regulation of interleukin-1 beta production / astrocyte activation / microglial cell activation / positive regulation of JNK cascade / positive regulation of smooth muscle cell proliferation / fibrillar center / positive regulation of inflammatory response / positive regulation of interleukin-6 production / positive regulation of non-canonical NF-kappaB signal transduction / neuron projection development / cellular response to amyloid-beta / positive regulation of neuron apoptotic process / positive regulation of reactive oxygen species metabolic process / positive regulation of fibroblast proliferation / signaling receptor activity / cell junction / amyloid-beta binding / positive regulation of NF-kappaB transcription factor activity / regulation of inflammatory response / membrane => GO:0016020 / positive regulation of ERK1 and ERK2 cascade / response to hypoxia / learning or memory / positive regulation of cell migration / inflammatory response / positive regulation of protein phosphorylation / positive regulation of apoptotic process / apical plasma membrane / axon / external side of plasma membrane / neuronal cell body / protein-containing complex binding / positive regulation of gene expression / cell surface / extracellular space / extracellular region / identical protein binding / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.503 Å | ||||||
Authors | Xu, D. / Young, J.H. / Krahn, J.M. / Song, D. / Corbett, K.D. / Chazin, W.J. / Pedersen, L.C. / Esko, J.D. | ||||||
Citation | Journal: Acs Chem.Biol. / Year: 2013 Title: Stable RAGE-Heparan Sulfate Complexes Are Essential for Signal Transduction. Authors: Xu, D. / Young, J.H. / Krahn, J.M. / Song, D. / Corbett, K.D. / Chazin, W.J. / Pedersen, L.C. / Esko, J.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4im8.cif.gz | 85.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4im8.ent.gz | 64.1 KB | Display | PDB format |
PDBx/mmJSON format | 4im8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/im/4im8 ftp://data.pdbj.org/pub/pdb/validation_reports/im/4im8 | HTTPS FTP |
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-Related structure data
Related structure data | 3cjjS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
#1: Protein | Mass: 22926.318 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ager, RAGE, mCG_5497 / Production host: Escherichia coli (E. coli) / References: UniProt: O35444, UniProt: Q62151*PLUS |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.82 Å3/Da / Density % sol: 56.43 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.1M Tris pH 8.5, 200mM MgCl2 and 22% PEG 400. Protein was purified on gel filtration in the presence of excess dodecasaccharide heparan sulfate that caused a shift in the elution profile ...Details: 0.1M Tris pH 8.5, 200mM MgCl2 and 22% PEG 400. Protein was purified on gel filtration in the presence of excess dodecasaccharide heparan sulfate that caused a shift in the elution profile from monomer to hexamer, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Aug 4, 2012 |
Radiation | Monochromator: Sagitally Focused Si 220 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.5→50 Å / Num. all: 3672 / Num. obs: 3672 / % possible obs: 99.5 % / Observed criterion σ(F): 48106 / Observed criterion σ(I): 48106 / Redundancy: 13.1 % / Rsym value: 0.107 / Net I/σ(I): 8.1 |
Reflection shell | Resolution: 3.5→3.63 Å / Redundancy: 12.2 % / Mean I/σ(I) obs: 4 / Num. unique all: 348 / Rsym value: 0.702 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3CJJ Resolution: 3.503→23.162 Å / SU ML: 0.39 / σ(F): 1.34 / Phase error: 36.42 / Stereochemistry target values: ML
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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: 3.503→23.162 Å
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Refine LS restraints |
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Refinement TLS params. | S33: 0 Å ° / Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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