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- PDB-2ggr: Solution structure of the C-terminal SH3 domain of c-CrkII -

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Basic information

Entry
Database: PDB / ID: 2ggr
TitleSolution structure of the C-terminal SH3 domain of c-CrkII
ComponentsProto-oncogene C-crk
KeywordsPROTEIN 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 / postsynaptic specialization assembly / protein phosphorylated amino acid binding / regulation of T cell migration / response to peptide / p130Cas linkage to MAPK signaling for integrins / regulation of dendrite development / positive regulation of skeletal muscle acetylcholine-gated channel clustering / reelin-mediated signaling pathway / 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 / regulation of GTPase activity / cellular response to insulin-like growth factor stimulus / establishment of cell polarity / 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 / ephrin receptor signaling pathway / cellular response to nitric oxide / positive regulation of substrate adhesion-dependent cell spreading / signaling adaptor activity / cellular response to transforming growth factor beta stimulus / insulin-like growth factor receptor binding / cytoskeletal protein binding / phosphotyrosine residue binding / ephrin receptor binding / protein tyrosine kinase binding / SH2 domain binding / cell chemotaxis / 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 / cerebral cortex development / receptor tyrosine kinase binding / SH3 domain binding / cell migration / actin cytoskeleton / signaling receptor complex adaptor activity / regulation of cell shape / protein-macromolecule adaptor activity / 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
CRK, N-terminal SH3 domain / CRK, C-terminal SH3 domain / : / Variant SH3 domain / SH3 Domains / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain ...CRK, N-terminal SH3 domain / CRK, C-terminal SH3 domain / : / Variant SH3 domain / SH3 Domains / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH3 type barrels. / Src homology 3 domains / SH2 domain superfamily / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Roll / Mainly Beta
Similarity search - Domain/homology
Adapter molecule crk
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / distance geometry simulated annealing
AuthorsMuralidharan, V. / Dutta, K. / Muir, T.W. / Cowburn, D.
CitationJournal: 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
DepositionMar 24, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 1, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_spectrometer ...database_2 / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.4May 29, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Proto-oncogene C-crk


Theoretical massNumber of molelcules
Total (without water)8,5301
Polymers8,5301
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 500structures with the least restraint violations,structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Proto-oncogene C-crk / P38 / Adapter molecule crk


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

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
1213D 15N-separated NOESY
1313D 13C aromatic NOESY
141HNHA
151HNCO 3J

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Sample preparation

DetailsContents: 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 conditionsIonic strength: 50mM / pH: 7.2 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE5001
Bruker AVANCEBrukerAVANCE7002
Bruker AVANCEBrukerAVANCE8003
Varian INOVAVarianINOVA6004

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Processing

NMR software
NameVersionDeveloperClassification
CNS1.1Brungerrefinement
ARIA2.2Nilgesstructure solution
RefinementMethod: distance geometry simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the least restraint violations,structures with the lowest energy
Conformers calculated total number: 500 / Conformers submitted total number: 20

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