+Open data
-Basic information
Entry | Database: PDB / ID: 2l3q | ||||||
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Title | Structure of the prolyl trans isomer of the Crk Protein | ||||||
Components | Trans isomer of Crk protein | ||||||
Keywords | STRUCTURAL PROTEIN / adapter protein | ||||||
Function / homology | Function and homology information ARMS-mediated activation / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / MET activates RAP1 and RAC1 / MET receptor recycling / Regulation of signaling by CBL / regulation of intracellular signal transduction / Regulation of actin dynamics for phagocytic cup formation / Downstream signal transduction / negative regulation of wound healing / p130Cas linkage to MAPK signaling for integrins ...ARMS-mediated activation / PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases / MET activates RAP1 and RAC1 / MET receptor recycling / Regulation of signaling by CBL / regulation of intracellular signal transduction / Regulation of actin dynamics for phagocytic cup formation / Downstream signal transduction / negative regulation of wound healing / p130Cas linkage to MAPK signaling for integrins / VEGFA-VEGFR2 Pathway / negative regulation of cell motility / regulation of GTPase activity / ephrin receptor signaling pathway / signaling adaptor activity / positive regulation of substrate adhesion-dependent cell spreading / phosphotyrosine residue binding / SH2 domain binding / ephrin receptor binding / regulation of actin cytoskeleton organization / receptor tyrosine kinase binding / SH3 domain binding / : / cell migration / regulation of cell shape / actin cytoskeleton organization / signal transduction / protein-containing complex / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Kalodimos, C. / Sarkar, P. / Saleh, T. / Tzeng, S. / Birge, R. | ||||||
Citation | Journal: Nat.Chem.Biol. / Year: 2011 Title: Structural basis for regulation of the Crk signaling protein by a proline switch. Authors: Sarkar, P. / Saleh, T. / Tzeng, S.R. / Birge, R.B. / Kalodimos, C.G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l3q.cif.gz | 530.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l3q.ent.gz | 450 KB | Display | PDB format |
PDBx/mmJSON format | 2l3q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l3/2l3q ftp://data.pdbj.org/pub/pdb/validation_reports/l3/2l3q | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8731.954 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Gene: CRK / Plasmid: pGex / Production host: Escherichia coli (E. coli) / References: UniProt: Q04929 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.6 mM [U-100% 13C; U-100% 15N] rtkh protein, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.6 mM / Component: rtkh protein / Isotopic labeling: [U-100% 13C; U-100% 15N] |
Sample conditions | Ionic strength: 0.140 / pH: 5.5 / Pressure: ambient / Temperature: 295 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software | Name: ARIA / Version: 1.2 / Developer: Linge, O'Donoghue and Nilges / Classification: refinement |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 20 |