+Open data
-Basic information
Entry | Database: PDB / ID: 2ggr | ||||||
---|---|---|---|---|---|---|---|
Title | Solution structure of the C-terminal SH3 domain of c-CrkII | ||||||
Components | Proto-oncogene C-crk | ||||||
Keywords | PROTEIN BINDING / solution structure / Crk-II / SH3 domain | ||||||
Function / homology | Function and homology information PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / ARMS-mediated activation / MET activates RAP1 and RAC1 / MET receptor recycling / response to hepatocyte growth factor / cellular response to endothelin / helper T cell diapedesis / cerebellar neuron development / response to cholecystokinin / regulation of leukocyte migration ...PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / ARMS-mediated activation / MET activates RAP1 and RAC1 / MET receptor recycling / response to hepatocyte growth factor / cellular response to endothelin / helper T cell diapedesis / cerebellar neuron development / response to cholecystokinin / regulation of leukocyte migration / Downstream signal transduction / response to peptide / postsynaptic specialization assembly / protein phosphorylated amino acid binding / regulation of T cell migration / p130Cas linkage to MAPK signaling for integrins / reelin-mediated signaling pathway / regulation of dendrite development / positive regulation of skeletal muscle acetylcholine-gated channel clustering / response to yeast / Regulation of signaling by CBL / regulation of Rac protein signal transduction / Regulation of actin dynamics for phagocytic cup formation / negative regulation of wound healing / negative regulation of natural killer cell mediated cytotoxicity / negative regulation of cell motility / VEGFA-VEGFR2 Pathway / protein localization to membrane / cellular response to insulin-like growth factor stimulus / establishment of cell polarity / regulation of GTPase activity / enzyme-linked receptor protein signaling pathway / positive regulation of smooth muscle cell migration / dendrite development / positive regulation of Rac protein signal transduction / regulation of cell adhesion mediated by integrin / cellular response to nitric oxide / ephrin receptor signaling pathway / signaling adaptor activity / positive regulation of substrate adhesion-dependent cell spreading / cellular response to transforming growth factor beta stimulus / insulin-like growth factor receptor binding / cytoskeletal protein binding / phosphotyrosine residue binding / SH2 domain binding / ephrin receptor binding / cell chemotaxis / protein tyrosine kinase binding / cellular response to nerve growth factor stimulus / hippocampus development / regulation of actin cytoskeleton organization / positive regulation of JNK cascade / neuron migration / neuromuscular junction / response to hydrogen peroxide / lipid metabolic process / receptor tyrosine kinase binding / cerebral cortex development / SH3 domain binding / : / signaling receptor complex adaptor activity / cell migration / actin cytoskeleton / protein-macromolecule adaptor activity / regulation of cell shape / actin cytoskeleton organization / scaffold protein binding / cell population proliferation / protein domain specific binding / ubiquitin protein ligase binding / enzyme binding / signal transduction / protein-containing complex / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing | ||||||
Authors | Muralidharan, V. / Dutta, K. / Muir, T.W. / Cowburn, D. | ||||||
Citation | Journal: Biochemistry / Year: 2006 Title: Solution Structure and Folding Characteristics of the C-Terminal SH3 Domain of c-Crk-II Authors: Muralidharan, V. / Dutta, K. / Cho, J. / Vila-Perello, M. / Raleigh, D.P. / Cowburn, D. / Muir, T.W. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2ggr.cif.gz | 395.3 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2ggr.ent.gz | 327.2 KB | Display | PDB format |
PDBx/mmJSON format | 2ggr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gg/2ggr ftp://data.pdbj.org/pub/pdb/validation_reports/gg/2ggr | HTTPS FTP |
---|
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 8529.591 Da / Num. of mol.: 1 / Fragment: C-terminal Domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Crk, Crko / Plasmid: pTrcHisA / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 / References: UniProt: Q64010 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 0.4 mM cSH3 domain U-15N,13C; 10mM phosphate buffer pH7.2; 50mM NaCl; 5mM DTT-d10; 0.1% NaN3; 1mM EDTA; 90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 50mM / pH: 7.2 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Radiation wavelength | Relative weight: 1 | |||||||||||||||||||||||||
NMR spectrometer |
|
-Processing
NMR software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 500 / Conformers submitted total number: 20 |