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- PDB-2mrk: Fyn SH2 domain in complex with the natural inhibitory phosphotyro... -

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Basic information

Entry
Database: PDB / ID: 2mrk
TitleFyn SH2 domain in complex with the natural inhibitory phosphotyrosine peptide
Components
  • C-terminal Tyrosine-protein kinase Fyn
  • Tyrosine-protein kinase Fyn
KeywordsTRANSFERASE / phosphorylated peptide / Fyn kinase / SH2 domain / Src kinase
Function / homology
Function and homology information


response to singlet oxygen / negative regulation of hydrogen peroxide biosynthetic process / Reelin signalling pathway / perinuclear endoplasmic reticulum / NTRK2 activates RAC1 / heart process / Activated NTRK2 signals through FYN / growth factor receptor binding / positive regulation of cysteine-type endopeptidase activity / regulation of glutamate receptor signaling pathway ...response to singlet oxygen / negative regulation of hydrogen peroxide biosynthetic process / Reelin signalling pathway / perinuclear endoplasmic reticulum / NTRK2 activates RAC1 / heart process / Activated NTRK2 signals through FYN / growth factor receptor binding / positive regulation of cysteine-type endopeptidase activity / regulation of glutamate receptor signaling pathway / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / regulation of calcium ion import across plasma membrane / negative regulation of dendritic spine maintenance / Platelet Adhesion to exposed collagen / CD28 co-stimulation / cellular response to L-glutamate / G protein-coupled glutamate receptor signaling pathway / FLT3 signaling through SRC family kinases / CRMPs in Sema3A signaling / positive regulation of protein localization to membrane / activated T cell proliferation / Nef and signal transduction / type 5 metabotropic glutamate receptor binding / feeding behavior / Nephrin family interactions / DCC mediated attractive signaling / EPH-Ephrin signaling / CD28 dependent Vav1 pathway / Ephrin signaling / dendrite morphogenesis / dendritic spine maintenance / Fc-gamma receptor signaling pathway involved in phagocytosis / Regulation of KIT signaling / leukocyte migration / CTLA4 inhibitory signaling / tau-protein kinase activity / phospholipase activator activity / EPHA-mediated growth cone collapse / Dectin-2 family / stimulatory C-type lectin receptor signaling pathway / cellular response to platelet-derived growth factor stimulus / PECAM1 interactions / response to amyloid-beta / CD28 dependent PI3K/Akt signaling / phospholipase binding / glial cell projection / Sema3A PAK dependent Axon repulsion / FCGR activation / cellular response to glycine / positive regulation of protein targeting to membrane / EPH-ephrin mediated repulsion of cells / ephrin receptor signaling pathway / alpha-tubulin binding / detection of mechanical stimulus involved in sensory perception of pain / Role of LAT2/NTAL/LAB on calcium mobilization / vascular endothelial growth factor receptor signaling pathway / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / cell surface receptor protein tyrosine kinase signaling pathway / regulation of peptidyl-tyrosine phosphorylation / positive regulation of tyrosine phosphorylation of STAT protein / cellular response to transforming growth factor beta stimulus / forebrain development / Signaling by ERBB2 / GPVI-mediated activation cascade / negative regulation of protein ubiquitination / T cell costimulation / EPHB-mediated forward signaling / ephrin receptor binding / CD209 (DC-SIGN) signaling / NCAM signaling for neurite out-growth / FCGR3A-mediated IL10 synthesis / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / learning / axon guidance / Regulation of signaling by CBL / actin filament / negative regulation of inflammatory response to antigenic stimulus / Cell surface interactions at the vascular wall / non-specific protein-tyrosine kinase / FCGR3A-mediated phagocytosis / non-membrane spanning protein tyrosine kinase activity / neuron migration / modulation of chemical synaptic transmission / protein catabolic process / tau protein binding / Signaling by SCF-KIT / negative regulation of protein catabolic process / Schaffer collateral - CA1 synapse / VEGFA-VEGFR2 Pathway / positive regulation of neuron projection development / peptidyl-tyrosine phosphorylation / positive regulation of protein localization to nucleus / cellular response to hydrogen peroxide / Signaling by CSF1 (M-CSF) in myeloid cells / Constitutive Signaling by Aberrant PI3K in Cancer / cellular response to amyloid-beta / calcium ion transport / disordered domain specific binding / PIP3 activates AKT signaling
Similarity search - Function
: / Fyn/Yrk, SH3 domain / SH2 domain / SHC Adaptor Protein / : / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain ...: / Fyn/Yrk, SH3 domain / SH2 domain / SHC Adaptor Protein / : / SH3 domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / Src homology 3 domains / SH2 domain superfamily / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Tyrosine-protein kinase Fyn
Similarity search - Component
Biological speciesHomo sapiens (human)
Homo Sapiens (human)
MethodSOLUTION NMR / simulated annealing, simulated annealing
Model detailsclosest to the average, model1
AuthorsHuculeci, R. / Buts, L. / Lenaerts, A.J. / van Nuland, N.
CitationJournal: Structure / Year: 2016
Title: Dynamically Coupled Residues within the SH2 Domain of FYN Are Key to Unlocking Its Activity.
Authors: Huculeci, R. / Cilia, E. / Lyczek, A. / Buts, L. / Houben, K. / Seeliger, M.A. / van Nuland, N. / Lenaerts, T.
History
DepositionJul 9, 2014Deposition site: BMRB / Processing site: RCSB
Revision 1.0Jul 15, 2015Provider: repository / Type: Initial release
Revision 1.1Oct 26, 2016Group: Database references
Revision 1.2Dec 14, 2016Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Tyrosine-protein kinase Fyn
B: C-terminal Tyrosine-protein kinase Fyn


Theoretical massNumber of molelcules
Total (without water)12,9452
Polymers12,9452
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area950 Å2
ΔGint-6 kcal/mol
Surface area6850 Å2
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)27 / 200structures with the lowest energy
RepresentativeModel #1closest to the average

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Components

#1: Protein Tyrosine-protein kinase Fyn / Proto-oncogene Syn / Proto-oncogene c-Fyn / Src-like kinase / SLK / p59-Fyn


Mass: 11690.341 Da / Num. of mol.: 1 / Fragment: UNP residues 149-248
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Description: The SH2 domain from human p59fyn is represented by residues 149-248.
Gene: FYN / Production host: Escherichia coli (E. coli)
References: UniProt: P06241, non-specific protein-tyrosine kinase
#2: Protein/peptide C-terminal Tyrosine-protein kinase Fyn / Proto-oncogene Syn / Proto-oncogene c-Fyn / Src-like kinase / SLK / p59-Fyn


Mass: 1254.195 Da / Num. of mol.: 1 / Fragment: UNP residues 528-537 / Source method: obtained synthetically
Details: The natural inhibitory peptide is a 10-residue phosphotyrosine segment from the C-terminal region of the Fyn kinase.
Source: (synth.) Homo Sapiens (human)
References: UniProt: P06241, non-specific protein-tyrosine kinase

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-1H NOESY
1212D 1H-1H TOCSY

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Sample preparation

DetailsContents: 0.93 mM [U-99% 13C; U-99% 15N] protein_1, 1.2 mM protein_2, 93% H2O/7% D2O
Solvent system: 93% H2O/7% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.93 mMentity_1-1[U-99% 13C; U-99% 15N]1
1.2 mMentity_2-21
Sample conditionsIonic strength: 0 / pH: 6.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian Varian NMR SystemsVarianVarian NMR Systems6001
Varian Varian NMR SystemsVarianVarian NMR Systems8002

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Processing

NMR software
NameDeveloperClassification
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
CCPNMRCCPNchemical shift assignment
CCPNMRCCPNpeak picking
HADDOCKAlexandre Bonvinstructure solution
HADDOCKAlexandre Bonvinrefinement
CNSBrunger, Adams, Clore, Gros, Nilges and Readstructure solution
CNSBrunger, Adams, Clore, Gros, Nilges and Readrefinement
RefinementMethod: simulated annealing, simulated annealing / Software ordinal: 1 / Details: HADDOCK runs under CNS
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 27

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