+Open data
-Basic information
Entry | Database: PDB / ID: 1f5x | ||||||
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Title | NMR STRUCTURE OF THE Y174 AUTOINHIBITED DBL HOMOLOGY DOMAIN | ||||||
Components | RHO-GEF VAV | ||||||
Keywords | SIGNALING PROTEIN / 11 alpha-HELICES | ||||||
Function / homology | Function and homology information Azathioprine ADME / CD28 dependent Vav1 pathway / RAC2 GTPase cycle / Erythropoietin activates RAS / GPVI-mediated activation cascade / RHOA GTPase cycle / FCERI mediated MAPK activation / NRAGE signals death through JNK / Signaling by SCF-KIT / RAC1 GTPase cycle ...Azathioprine ADME / CD28 dependent Vav1 pathway / RAC2 GTPase cycle / Erythropoietin activates RAS / GPVI-mediated activation cascade / RHOA GTPase cycle / FCERI mediated MAPK activation / NRAGE signals death through JNK / Signaling by SCF-KIT / RAC1 GTPase cycle / RHOG GTPase cycle / VEGFR2 mediated vascular permeability / FCERI mediated Ca+2 mobilization / phosphorylation-dependent protein binding / G alpha (12/13) signalling events / PIP3 activates AKT signaling / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / Regulation of signaling by CBL / Regulation of actin dynamics for phagocytic cup formation / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Interleukin-3, Interleukin-5 and GM-CSF signaling / VEGFA-VEGFR2 Pathway / regulation of cell size / positive regulation of natural killer cell mediated cytotoxicity / T cell differentiation / positive regulation of cell adhesion / phagocytosis / reactive oxygen species metabolic process / phosphotyrosine residue binding / T cell activation / guanyl-nucleotide exchange factor activity / neutrophil chemotaxis / integrin-mediated signaling pathway / cell-cell junction / cell migration / intracellular signal transduction / immune response / G protein-coupled receptor signaling pathway / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Aghazadeh, B. / Rosen, M.K. / Lowry, W.E. / Huang, X.Y. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2000 Title: Structural basis for relief of autoinhibition of the Dbl homology domain of proto-oncogene Vav by tyrosine phosphorylation. Authors: Aghazadeh, B. / Lowry, W.E. / Huang, X.Y. / Rosen, M.K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1f5x.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1f5x.ent.gz | 1.1 MB | Display | PDB format |
PDBx/mmJSON format | 1f5x.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/f5/1f5x ftp://data.pdbj.org/pub/pdb/validation_reports/f5/1f5x | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 24490.309 Da / Num. of mol.: 1 / Fragment: DBL HOMOLOGY DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PET11A / Production host: Escherichia coli (E. coli) / References: UniProt: P27870 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using 3D and 4D heteronuclear techniques on deuterated samples in conjunction with selective methyl and aromatic labeling |
-Sample preparation
Details | Contents: 1.4 mM 15N,13C,2H; 20 mM phosphate buffer; 50 mM NaCl; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 70 mM / pH: 7 / Pressure: ambient / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: CNS was used in the initial global fold determination. High-resolution structures were obtained using ARIA. Final structures are based on a total of 3966 restraints, 3523 are NOE-derived ...Details: CNS was used in the initial global fold determination. High-resolution structures were obtained using ARIA. Final structures are based on a total of 3966 restraints, 3523 are NOE-derived distance constraints, 443 dihedral angle restraints, 96 distance restraints | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 20 / Conformers submitted total number: 20 |