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- PDB-4jeg: Crystal Structure of Monobody CS1/SHP2 C-SH2 Domain Complex -

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Basic information

Entry
Database: PDB / ID: 4jeg
TitleCrystal Structure of Monobody CS1/SHP2 C-SH2 Domain Complex
Components
  • Monobody CS1
  • Tyrosine-protein phosphatase non-receptor type 11
KeywordsSignaling protein/protein binding / engineered binding protein / SHP2 SH2-monobody complex / Phosphatase / Phosphotyrosine Binding / Phosphorylation / Signaling protein-protein binding complex
Function / homology
Function and homology information


negative regulation of monocyte activation / calcium-independent cell-matrix adhesion / negative regulation of transforming growth factor beta production / Fibronectin matrix formation / negative regulation of cortisol secretion / intestinal epithelial cell migration / microvillus organization / negative regulation of growth hormone secretion / Extracellular matrix organization / positive regulation of substrate-dependent cell migration, cell attachment to substrate ...negative regulation of monocyte activation / calcium-independent cell-matrix adhesion / negative regulation of transforming growth factor beta production / Fibronectin matrix formation / negative regulation of cortisol secretion / intestinal epithelial cell migration / microvillus organization / negative regulation of growth hormone secretion / Extracellular matrix organization / positive regulation of substrate-dependent cell migration, cell attachment to substrate / genitalia development / neural crest cell migration involved in autonomic nervous system development / atrioventricular canal development / peptidase activator activity / fibrinogen complex / negative regulation of cell adhesion mediated by integrin / peptide cross-linking / STAT5 Activation / Netrin mediated repulsion signals / integrin activation / positive regulation of hormone secretion / cerebellar cortex formation / ALK mutants bind TKIs / multicellular organismal reproductive process / cell-substrate junction assembly / regulation of protein export from nucleus / positive regulation of ossification / hormone metabolic process / Interleukin-37 signaling / negative regulation of chondrocyte differentiation / Signaling by Leptin / MET activates PTPN11 / Regulation of RUNX1 Expression and Activity / face morphogenesis / biological process involved in interaction with symbiont / ERBB signaling pathway / Molecules associated with elastic fibres / Costimulation by the CD28 family / proteoglycan binding / Signal regulatory protein family interactions / peptide hormone receptor binding / triglyceride metabolic process / platelet formation / negative regulation of type I interferon production / extracellular matrix structural constituent / MET activates PTK2 signaling / megakaryocyte development / Syndecan interactions / organ growth / CTLA4 inhibitory signaling / Platelet sensitization by LDL / Interleukin-20 family signaling / PI-3K cascade:FGFR3 / Interleukin-6 signaling / p130Cas linkage to MAPK signaling for integrins / STAT5 activation downstream of FLT3 ITD mutants / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR4 / Prolactin receptor signaling / PI-3K cascade:FGFR1 / endodermal cell differentiation / MAPK3 (ERK1) activation / phosphoprotein phosphatase activity / inner ear development / MAPK1 (ERK2) activation / PECAM1 interactions / Bergmann glial cell differentiation / regulation of cell adhesion mediated by integrin / neurotrophin TRK receptor signaling pathway / regulation of type I interferon-mediated signaling pathway / GRB2:SOS provides linkage to MAPK signaling for Integrins / platelet-derived growth factor receptor signaling pathway / non-membrane spanning protein tyrosine phosphatase activity / Signaling by ALK fusions and activated point mutants / Non-integrin membrane-ECM interactions / RET signaling / peptidyl-tyrosine dephosphorylation / basement membrane / Interleukin-3, Interleukin-5 and GM-CSF signaling / PI3K Cascade / Regulation of IFNA/IFNB signaling / endoplasmic reticulum-Golgi intermediate compartment / ECM proteoglycans / PD-1 signaling / negative regulation of insulin secretion / ephrin receptor signaling pathway / regulation of protein-containing complex assembly / fibroblast growth factor receptor signaling pathway / positive regulation of axon extension / GAB1 signalosome / Integrin cell surface interactions / Activated NTRK2 signals through FRS2 and FRS3 / Nuclear events stimulated by ALK signaling in cancer / Regulation of IFNG signaling / positive regulation of insulin receptor signaling pathway / homeostasis of number of cells within a tissue / FRS-mediated FGFR3 signaling / Signaling by CSF3 (G-CSF) / Signaling by FLT3 ITD and TKD mutants / FRS-mediated FGFR2 signaling
Similarity search - Function
Fibronectin type I domain / Fibronectin, type I / Fibronectin type-I domain signature. / Fibronectin type-I domain profile. / Fibronectin type 1 domain / Protein-tyrosine phosphatase, non-receptor type-6, -11 / Fibronectin type II domain / Fibronectin type II domain superfamily / Fibronectin type II domain / Fibronectin type-II collagen-binding domain signature. ...Fibronectin type I domain / Fibronectin, type I / Fibronectin type-I domain signature. / Fibronectin type-I domain profile. / Fibronectin type 1 domain / Protein-tyrosine phosphatase, non-receptor type-6, -11 / Fibronectin type II domain / Fibronectin type II domain superfamily / Fibronectin type II domain / Fibronectin type-II collagen-binding domain signature. / Fibronectin type-II collagen-binding domain profile. / Fibronectin type 2 domain / SH2 domain / SHC Adaptor Protein / Protein tyrosine phosphatase, catalytic domain / PTP type protein phosphatase domain profile. / Protein-tyrosine phosphatase / Tyrosine-specific protein phosphatase, PTPase domain / Protein-tyrosine phosphatase, catalytic / Protein tyrosine phosphatase, catalytic domain motif / Tyrosine specific protein phosphatases active site. / Protein-tyrosine phosphatase, active site / Kringle-like fold / Tyrosine-specific protein phosphatases domain / Tyrosine specific protein phosphatases domain profile. / Protein-tyrosine phosphatase-like / EGF-like domain signature 1. / Fibronectin type III domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Fibronectin / Tyrosine-protein phosphatase non-receptor type 11
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.3 Å
AuthorsSha, F. / Koide, S.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2013
Title: Dissection of the BCR-ABL signaling network using highly specific monobody inhibitors to the SHP2 SH2 domains.
Authors: Sha, F. / Gencer, E.B. / Georgeon, S. / Koide, A. / Yasui, N. / Koide, S. / Hantschel, O.
History
DepositionFeb 26, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 28, 2013Provider: repository / Type: Initial release
Revision 1.1Sep 11, 2013Group: Database references
Revision 1.2Sep 25, 2013Group: Database references
Revision 1.3Nov 20, 2013Group: Data collection
Revision 1.4Mar 12, 2014Group: Structure summary

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Tyrosine-protein phosphatase non-receptor type 11
B: Monobody CS1


Theoretical massNumber of molelcules
Total (without water)24,4772
Polymers24,4772
Non-polymers00
Water1,44180
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2110 Å2
ΔGint-11 kcal/mol
Surface area10480 Å2
MethodPISA
Unit cell
Length a, b, c (Å)111.700, 111.700, 31.780
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number169
Space group name H-MP61

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Components

#1: Protein Tyrosine-protein phosphatase non-receptor type 11 / Protein-tyrosine phosphatase 1D / PTP-1D / Protein-tyrosine phosphatase 2C / PTP-2C / SH-PTP2 / SHP- ...Protein-tyrosine phosphatase 1D / PTP-1D / Protein-tyrosine phosphatase 2C / PTP-2C / SH-PTP2 / SHP-2 / Shp2 / SH-PTP3


Mass: 14006.806 Da / Num. of mol.: 1 / Fragment: C-terminal SH2 domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PTP2C, PTPN11, SHPTP2 / Plasmid: pHBT / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q06124
#2: Protein Monobody CS1


Mass: 10470.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pHFT2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P02751*PLUS
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 80 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.34 Å3/Da / Density % sol: 47.39 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 25% PEG 3350, 0.1M Bis-tris, 0.2M Sodium Chloride, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 20, 2012
RadiationMonochromator: Si(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.3→19.35 Å / Num. all: 10400 / Num. obs: 10358 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 3 / Redundancy: 7.9 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 21.2
Reflection shellResolution: 2.3→2.42 Å / Redundancy: 7.4 % / Rmerge(I) obs: 0.423 / Mean I/σ(I) obs: 4.4 / Num. unique all: 1503 / % possible all: 99.6

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
PHASERphasing
PHENIX1.7.3_928refinement
PDB_EXTRACT3.11data extraction
ADSCQuantumdata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3→19.347 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.8461 / SU ML: 0.26 / σ(F): 1.44 / Phase error: 22.11 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2268 498 4.81 %random
Rwork0.1868 ---
obs0.1888 10352 99.78 %-
all-10375 --
Solvent computationShrinkage radii: 0.6 Å / VDW probe radii: 0.9 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 40.722 Å2 / ksol: 0.404 e/Å3
Displacement parametersBiso max: 103.27 Å2 / Biso mean: 34.5368 Å2 / Biso min: 10.39 Å2
Baniso -1Baniso -2Baniso -3
1--0.2239 Å20 Å2-0 Å2
2---0.2239 Å20 Å2
3---0.4479 Å2
Refinement stepCycle: LAST / Resolution: 2.3→19.347 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1638 0 0 80 1718
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0041682
X-RAY DIFFRACTIONf_angle_d0.8852284
X-RAY DIFFRACTIONf_chiral_restr0.062249
X-RAY DIFFRACTIONf_plane_restr0.004287
X-RAY DIFFRACTIONf_dihedral_angle_d14.989605
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 4

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.3-2.52990.31411150.2372420253599
2.5299-2.89490.30471320.215824412573100
2.8949-3.64330.20681300.177224422572100
3.6433-19.34770.18631210.168325512672100

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