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- PDB-1bfj: SOLUTION STRUCTURE OF THE C-TERMINAL SH2 DOMAIN OF THE P85ALPHA R... -

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Database: PDB / ID: 1bfj
TitleSOLUTION STRUCTURE OF THE C-TERMINAL SH2 DOMAIN OF THE P85ALPHA REGULATORY SUBUNIT OF PHOSPHOINOSITIDE 3-KINASE, NMR, MINIMIZED AVERAGE STRUCTURE
ComponentsP85 ALPHA
KeywordsSH2 DOMAIN / P85ALPHA / PI 3-KINASE / C TERMINAL SH2 DOMAIN
Function / homology
Function and homology information


RHOC GTPase cycle / PI3K events in ERBB4 signaling / Interleukin-7 signaling / GAB1 signalosome / PI3K events in ERBB2 signaling / MET activates PI3K/AKT signaling / CDC42 GTPase cycle / RHOD GTPase cycle / RHOJ GTPase cycle / RAC3 GTPase cycle ...RHOC GTPase cycle / PI3K events in ERBB4 signaling / Interleukin-7 signaling / GAB1 signalosome / PI3K events in ERBB2 signaling / MET activates PI3K/AKT signaling / CDC42 GTPase cycle / RHOD GTPase cycle / RHOJ GTPase cycle / RAC3 GTPase cycle / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / FLT3 Signaling / RND2 GTPase cycle / RND1 GTPase cycle / IRS-mediated signalling / GPVI-mediated activation cascade / Signaling by SCF-KIT / Downstream signal transduction / PI3K/AKT activation / Signaling by ALK / Role of phospholipids in phagocytosis / Tie2 Signaling / Role of LAT2/NTAL/LAB on calcium mobilization / Costimulation by the CD28 family / CD28 dependent PI3K/Akt signaling / RAC1 GTPase cycle / RAC2 GTPase cycle / Interleukin receptor SHC signaling / RND3 GTPase cycle / PI-3K cascade:FGFR1 / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR3 / PI-3K cascade:FGFR4 / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / PI3K Cascade / PIP3 activates AKT signaling / GP1b-IX-V activation signalling / RAF/MAP kinase cascade / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / Synthesis of PIPs at the plasma membrane / RHOA GTPase cycle / RHOF GTPase cycle / DAP12 signaling / RHOU GTPase cycle / RHOV GTPase cycle / Regulation of signaling by CBL / Downstream TCR signaling / RHOG GTPase cycle / RET signaling / Interleukin-3, Interleukin-5 and GM-CSF signaling / VEGFA-VEGFR2 Pathway / phosphatidylinositol 3-kinase regulator activity / phosphatidylinositol 3-kinase activator activity / 1-phosphatidylinositol-3-kinase regulator activity / ErbB-3 class receptor binding / transmembrane receptor protein tyrosine kinase adaptor activity / positive regulation of endoplasmic reticulum unfolded protein response / phosphatidylinositol 3-kinase complex, class IA / phosphatidylinositol 3-kinase complex / enzyme-substrate adaptor activity / Extra-nuclear estrogen signaling / G alpha (q) signalling events / intracellular glucose homeostasis / phosphatidylinositol phosphate biosynthetic process / insulin receptor substrate binding / phosphatidylinositol 3-kinase binding / insulin-like growth factor receptor binding / phosphatidylinositol 3-kinase/protein kinase B signal transduction / response to endoplasmic reticulum stress / substrate adhesion-dependent cell spreading / insulin-like growth factor receptor signaling pathway / positive regulation of RNA splicing / positive regulation of D-glucose import / positive regulation of protein localization to plasma membrane / insulin receptor binding / positive regulation of protein import into nucleus / cellular response to insulin stimulus / protein transport / insulin receptor signaling pathway / protein stabilization / negative regulation of apoptotic process / positive regulation of transcription by RNA polymerase II / identical protein binding / nucleus
Similarity search - Function
Phosphatidylinositol 3-kinase regulatory subunit alpha, SH3 domain / PIK3R1, inter-SH2 domain / PI3K p85 subunit, C-terminal SH2 domain / PI3K regulatory subunit p85-related , inter-SH2 domain / PI3K p85 subunit, N-terminal SH2 domain / Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases ...Phosphatidylinositol 3-kinase regulatory subunit alpha, SH3 domain / PIK3R1, inter-SH2 domain / PI3K p85 subunit, C-terminal SH2 domain / PI3K regulatory subunit p85-related , inter-SH2 domain / PI3K p85 subunit, N-terminal SH2 domain / Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases / Rho GTPase activation protein / SH2 domain / SHC Adaptor Protein / 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 / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Phosphatidylinositol 3-kinase regulatory subunit alpha
Similarity search - Component
Biological speciesBos taurus (cattle)
MethodSOLUTION NMR / simulated annealing
AuthorsSiegal, G. / Davis, B. / Kristensen, S.M. / Sankar, A. / Linacre, J. / Stein, R.C. / Panayotou, G. / Waterfield, M.D. / Driscoll, P.C.
CitationJournal: J.Mol.Biol. / Year: 1998
Title: Solution structure of the C-terminal SH2 domain of the p85 alpha regulatory subunit of phosphoinositide 3-kinase.
Authors: Siegal, G. / Davis, B. / Kristensen, S.M. / Sankar, A. / Linacre, J. / Stein, R.C. / Panayotou, G. / Waterfield, M.D. / Driscoll, P.C.
History
DepositionNov 18, 1997Processing site: BNL
Revision 1.0Feb 25, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4May 22, 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: P85 ALPHA


Theoretical massNumber of molelcules
Total (without water)12,7461
Polymers12,7461
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)1 / 100NO NOE VIOLATION > 0.3A, NO DIHEDRAL VIOLATION > 3.0
Representative

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Components

#1: Protein P85 ALPHA / PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY ALPHA SUBUNIT / PI3-KINASE P85-ALPHA SUBUNIT


Mass: 12746.247 Da / Num. of mol.: 1 / Fragment: C TERMINAL SH2 DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (cattle) / Cell line: BL21 / Organ: BRAIN / Plasmid: BL21 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P23727

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: VARIOUS

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Sample preparation

Sample conditionsIonic strength: 50 mM / pH: 7.5 / Pressure: 1 atm / Temperature: 290 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.84model building
X-PLOR3.84refinement
X-PLOR3.84phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.84BRUNGERrefinement
XPLORstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
Details: 30 CONFORMERS WERE DETERMINED BY RESTRAINED MOLECULAR DYNAMICS/SIMULATED ANNEALING METHOD USING THE PROGRAM X-PLOR 3.84. THE STRUCTURES ARE BASED ON 1908 INTERPROTON DISTANCE RESTRAINTS ...Details: 30 CONFORMERS WERE DETERMINED BY RESTRAINED MOLECULAR DYNAMICS/SIMULATED ANNEALING METHOD USING THE PROGRAM X-PLOR 3.84. THE STRUCTURES ARE BASED ON 1908 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 88 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 44 HYDROGEN-BONDS IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON EXCHANGE DATA; 25 TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING CONSTANTS AND NOE DATA. THE RMS DISTRIBUTION ABOUT THE MEAN COORDINATE POSITIONS IS 0.57 ANGSTROMS FOR ALL BACKBONE ATOMS AND 1.12 ANGSTROMS FOR ALL ATOMS. THE AVERAGE STRUCTURE WAS THEN CALCULATED BY BEST FIT SUPERPOSITION, COORDINATE AVERAGING AND RESTRAINED ENERGY MINIMIZATION.
NMR ensembleConformer selection criteria: NO NOE VIOLATION > 0.3A, NO DIHEDRAL VIOLATION > 3.0
Conformers calculated total number: 100 / Conformers submitted total number: 1

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