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- PDB-1m3c: Solution structure of a circular form of the N-terminal SH3 domai... -
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Basic information
Entry | Database: PDB / ID: 1m3c | ||||||
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Title | Solution structure of a circular form of the N-terminal SH3 domain (E132C, E133G, R191G mutant) from oncogene protein c-Crk | ||||||
![]() | Proto-oncogene C-crk | ||||||
![]() | PROTEIN BINDING / SH3 / SH3 DOMAIN / CIRCULAR PROTEIN / CYCLIZED PROTEIN / ADAPTOR PROTEIN | ||||||
Function / homology | ![]() 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 / postsynaptic specialization assembly / protein phosphorylated amino acid binding / response to peptide / 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 / negative regulation of natural killer cell mediated cytotoxicity / response to yeast / Regulation of signaling by CBL / Regulation of actin dynamics for phagocytic cup formation / regulation of Rac protein signal transduction / negative regulation of wound healing / negative regulation of cell motility / protein localization to membrane / VEGFA-VEGFR2 Pathway / 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 / ephrin receptor binding / phosphotyrosine residue binding / SH2 domain 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 / response to hydrogen peroxide / neuromuscular junction / lipid metabolic process / receptor tyrosine kinase binding / cerebral cortex development / SH3 domain binding / actin cytoskeleton / signaling receptor complex adaptor activity / cell migration / 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 / protein-containing complex / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / Simulated annealing, torsion angle dynamics | ||||||
![]() | Schumann, F.H. / Varadan, R. / Tayakuniyil, P.P. / Hall, J.B. / Camarero, J.A. / Fushman, D. | ||||||
![]() | ![]() Title: Changing protein backbone topology: Structural and dynamic consequences of the backbone cyclization in SH3 domain Authors: Schumann, F.H. / Varadan, R. / Tayakuniyil, P.P. / Hall, J.B. / Camarero, J.A. / Fushman, D. #1: ![]() Title: Rescuing a destabilized protein fold through backbone cyclization Authors: Camarero, J.A. / Fushman, D. / Sato, S. / Giriat, I. / Cowburn, D. / Raleigh, D.P. / Muir, T.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 374.1 KB | Display | ![]() |
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PDB format | ![]() | 323.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 7031.783 Da / Num. of mol.: 1 / Fragment: N-TERMINAL SH3 DOMAIN (residues 132-191) / Mutation: R191G, added G133, C132 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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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 standard 2D homonuclear techniques combined with 2D 1H-15N HSQC data. |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 100 mM NaCl / pH: 7.2 / Pressure: ambient / Temperature: 307 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: Simulated annealing, torsion angle dynamics / Software ordinal: 1 Details: The structures are based on 1010 restraints, 913 are NOE-derived distance contraints, 25 dihedral angle constraints, and 72 distance restraints from hydrogen bonds. Structures were ...Details: The structures are based on 1010 restraints, 913 are NOE-derived distance contraints, 25 dihedral angle constraints, and 72 distance restraints from hydrogen bonds. Structures were calculated using program DYANA. No further refinement was performed. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest target function | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest target function Conformers calculated total number: 200 / Conformers submitted total number: 20 |