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Yorodumi- PDB-2fjl: Solution Structure of the Split PH domain in Phospholipase C-gamma1 -
+Open data
-Basic information
Entry | Database: PDB / ID: 2fjl | ||||||
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Title | Solution Structure of the Split PH domain in Phospholipase C-gamma1 | ||||||
Components | 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma 1 | ||||||
Keywords | HYDROLASE / beta-barrel | ||||||
Function / homology | Function and homology information PECAM1 interactions / EGFR interacts with phospholipase C-gamma / Activated NTRK2 signals through PLCG1 / Activated NTRK3 signals through PLCG1 / phosphatidylinositol catabolic process / Phospholipase C-mediated cascade: FGFR1 / Phospholipase C-mediated cascade; FGFR3 / Phospholipase C-mediated cascade; FGFR4 / ISG15 antiviral mechanism / Generation of second messenger molecules ...PECAM1 interactions / EGFR interacts with phospholipase C-gamma / Activated NTRK2 signals through PLCG1 / Activated NTRK3 signals through PLCG1 / phosphatidylinositol catabolic process / Phospholipase C-mediated cascade: FGFR1 / Phospholipase C-mediated cascade; FGFR3 / Phospholipase C-mediated cascade; FGFR4 / ISG15 antiviral mechanism / Generation of second messenger molecules / Phospholipase C-mediated cascade; FGFR2 / Downstream signal transduction / Signaling by ALK / Role of phospholipids in phagocytosis / inositol trisphosphate biosynthetic process / DAP12 signaling / FCERI mediated Ca+2 mobilization / VEGFR2 mediated cell proliferation / calcium-dependent phospholipase C activity / Synthesis of IP3 and IP4 in the cytosol / RET signaling / inositol trisphosphate metabolic process / response to curcumin / phosphoinositide phospholipase C / FCERI mediated MAPK activation / response to gravity / phosphatidylinositol metabolic process / phosphatidylinositol phospholipase C activity / COP9 signalosome / phospholipase C activity / neurotrophin TRKA receptor binding / positive regulation of endothelial cell apoptotic process / clathrin-coated vesicle / positive regulation of vascular endothelial cell proliferation / positive regulation of epithelial cell migration / phosphatidylinositol-mediated signaling / cellular response to epidermal growth factor stimulus / positive regulation of blood vessel endothelial cell migration / glutamate receptor binding / release of sequestered calcium ion into cytosol / ruffle / : / positive regulation of release of sequestered calcium ion into cytosol / guanyl-nucleotide exchange factor activity / epidermal growth factor receptor signaling pathway / cell projection / phosphoprotein binding / ruffle membrane / calcium-mediated signaling / insulin receptor binding / modulation of chemical synaptic transmission / response to hydrogen peroxide / Schaffer collateral - CA1 synapse / receptor tyrosine kinase binding / positive regulation of angiogenesis / calcium ion transport / cell-cell junction / cell migration / lamellipodium / T cell receptor signaling pathway / in utero embryonic development / glutamatergic synapse / calcium ion binding / protein kinase binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Wen, W. / Zhang, M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2006 Title: Structural Characterization of the Split Pleckstrin Homology Domain in Phospholipase C-{gamma}1 and Its Interaction with TRPC3 Authors: Wen, W. / Yan, J. / Zhang, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2fjl.cif.gz | 681.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2fjl.ent.gz | 570.8 KB | Display | PDB format |
PDBx/mmJSON format | 2fjl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fj/2fjl ftp://data.pdbj.org/pub/pdb/validation_reports/fj/2fjl | 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: 16915.568 Da / Num. of mol.: 1 / Fragment: the Split PH2 domain, residuse 1-35 and 112-148 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: pET32a / Production host: Escherichia coli (E. coli) References: UniProt: P10686, phosphoinositide phospholipase C |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details |
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Sample conditions | pH: 6.5 / Pressure: ambient / Temperature: 308 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software | Name: CNS / Version: 1.1 / Developer: Brunger / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: the structures are based on a total of 2145 restraints, 2023 are NOE-derived distance constraints, 60 dihedral angle restraints,62 distance restraints from hydrogen bonds. |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 15 |