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Yorodumi- PDB-1jeg: Solution structure of the SH3 domain from C-terminal Src Kinase c... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1jeg | ||||||
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Title | Solution structure of the SH3 domain from C-terminal Src Kinase complexed with a peptide from the tyrosine phosphatase PEP | ||||||
Components |
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Keywords | TRANSFERASE/HYDROLASE / SH3 domain / protein-peptide complex / tyrosine phosphatase / kinase / TRANSFERASE-HYDROLASE COMPLEX | ||||||
Function / homology | Function and homology information phosphoanandamide dephosphorylation / negative regulation of Golgi to plasma membrane protein transport / positive regulation of granzyme B production / GAB1 signalosome / positive regulation of toll-like receptor 3 signaling pathway / Phosphorylation of CD3 and TCR zeta chains / Translocation of ZAP-70 to Immunological synapse / regulation of leukocyte migration / regulation of Fc receptor mediated stimulatory signaling pathway / regulation of natural killer cell proliferation ...phosphoanandamide dephosphorylation / negative regulation of Golgi to plasma membrane protein transport / positive regulation of granzyme B production / GAB1 signalosome / positive regulation of toll-like receptor 3 signaling pathway / Phosphorylation of CD3 and TCR zeta chains / Translocation of ZAP-70 to Immunological synapse / regulation of leukocyte migration / regulation of Fc receptor mediated stimulatory signaling pathway / regulation of natural killer cell proliferation / negative regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway / PD-1 signaling / positive regulation of toll-like receptor 7 signaling pathway / Integrin signaling / MAP2K and MAPK activation / negative regulation of p38MAPK cascade / positive regulation of toll-like receptor 4 signaling pathway / positive regulation of toll-like receptor 9 signaling pathway / regulation of non-canonical NF-kappaB signal transduction / negative regulation of T cell activation / negative regulation of low-density lipoprotein particle clearance / positive regulation of protein K63-linked ubiquitination / cellular response to muramyl dipeptide / negative regulation of interleukin-8 production / negative regulation of JUN kinase activity / regulation of calcium ion transmembrane transport / proline-rich region binding / negative regulation of bone resorption / adherens junction organization / negative regulation of phagocytosis / regulation of T cell activation / cellular response to peptide hormone stimulus / negative regulation of T cell receptor signaling pathway / negative regulation of kinase activity / positive regulation of CD8-positive, alpha-beta T cell proliferation / oligodendrocyte differentiation / phosphatase activity / protein kinase A catalytic subunit binding / negative regulation of interleukin-6 production / negative regulation of tumor necrosis factor production / non-membrane spanning protein tyrosine phosphatase activity / T cell differentiation / peptidyl-tyrosine dephosphorylation / positive regulation of type I interferon production / positive regulation of interferon-alpha production / regulation of peptidyl-tyrosine phosphorylation / lipopolysaccharide-mediated signaling pathway / positive regulation of defense response to virus by host / positive regulation of interferon-beta production / negative regulation of autophagy / protein dephosphorylation / protein-tyrosine-phosphatase / protein tyrosine kinase binding / protein tyrosine phosphatase activity / non-specific protein-tyrosine kinase / positive regulation of MAP kinase activity / non-membrane spanning protein tyrosine kinase activity / brain development / negative regulation of ERK1 and ERK2 cascade / cytoplasmic side of plasma membrane / autophagy / kinase binding / positive regulation of protein import into nucleus / SH3 domain binding / positive regulation of type II interferon production / cell-cell junction / T cell receptor signaling pathway / transferase activity / protein phosphatase binding / protein tyrosine kinase activity / adaptive immune response / response to lipopolysaccharide / protein autophosphorylation / positive regulation of ERK1 and ERK2 cascade / intracellular signal transduction / membrane raft / negative regulation of cell population proliferation / protein phosphorylation / negative regulation of gene expression / ubiquitin protein ligase binding / positive regulation of gene expression / perinuclear region of cytoplasm / ATP binding / identical protein binding / nucleus / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / simulated annealing, torsional angle dynmaics | ||||||
Authors | Ghose, R. / Shekhtman, A. / Goger, M.J. / Ji, H. / Cowburn, D. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2001 Title: A novel, specific interaction involving the Csk SH3 domain and its natural ligand. Authors: Ghose, R. / Shekhtman, A. / Goger, M.J. / Ji, H. / Cowburn, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jeg.cif.gz | 588 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jeg.ent.gz | 491.1 KB | Display | PDB format |
PDBx/mmJSON format | 1jeg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1jeg_validation.pdf.gz | 354.8 KB | Display | wwPDB validaton report |
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Full document | 1jeg_full_validation.pdf.gz | 727.7 KB | Display | |
Data in XML | 1jeg_validation.xml.gz | 43.8 KB | Display | |
Data in CIF | 1jeg_validation.cif.gz | 67.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/je/1jeg ftp://data.pdbj.org/pub/pdb/validation_reports/je/1jeg | HTTPS FTP |
-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: 9198.627 Da / Num. of mol.: 1 / Fragment: SH3 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / References: UniProt: P41241, EC: 2.7.1.112 |
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#2: Protein/peptide | Mass: 2912.187 Da / Num. of mol.: 1 / Fragment: 25 residue peptide (residues 612-629) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / References: UniProt: P29352, protein-tyrosine-phosphatase |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Sample conditions | pH: 7.2 / Pressure: 1 atm / Temperature: 293 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsional angle dynmaics / Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 1000 / Conformers submitted total number: 25 |