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- PDB-1qg1: GROWTH FACTOR RECEPTOR BINDING PROTEIN SH2 DOMAIN COMPLEXED WITH ... -

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Basic information

Entry
Database: PDB / ID: 1qg1
TitleGROWTH FACTOR RECEPTOR BINDING PROTEIN SH2 DOMAIN COMPLEXED WITH AN SHC-DERIVED PEPTIDE
Components
  • PROTEIN (GROWTH FACTOR RECEPTOR BINDING PROTEIN)
  • PROTEIN (SHC-DERIVED PEPTIDE)
KeywordsHORMONE/GROWTH FACTOR / SIGNAL TRANSDUCTION / SH2 DOMAIN / PHOSPHOTYROSYL PEPTIDE / COMPLEX (SIGNAL TRANSDUCTION-PEPTIDE) / HORMONE-GROWTH FACTOR COMPLEX
Function / homology
Function and homology information


regulation of superoxide metabolic process / positive regulation of cell proliferation in bone marrow / guanyl-nucleotide exchange factor adaptor activity / Grb2-EGFR complex / branching involved in labyrinthine layer morphogenesis / XBP1(S) activates chaperone genes / STAT5 Activation / COP9 signalosome / vesicle membrane / neurotrophin TRKA receptor binding ...regulation of superoxide metabolic process / positive regulation of cell proliferation in bone marrow / guanyl-nucleotide exchange factor adaptor activity / Grb2-EGFR complex / branching involved in labyrinthine layer morphogenesis / XBP1(S) activates chaperone genes / STAT5 Activation / COP9 signalosome / vesicle membrane / neurotrophin TRKA receptor binding / Activated NTRK2 signals through PI3K / MET receptor recycling / transmembrane receptor protein tyrosine kinase adaptor activity / Signaling by cytosolic FGFR1 fusion mutants / Interleukin-15 signaling / MET activates PTPN11 / MET activates RAP1 and RAC1 / Shc-EGFR complex / Interleukin-2 signaling / CD28 dependent Vav1 pathway / Costimulation by the CD28 family / MET activates PI3K/AKT signaling / epidermal growth factor binding / Signal regulatory protein family interactions / Regulation of KIT signaling / epidermal growth factor receptor binding / Signaling by ALK / positive regulation of actin filament polymerization / PI-3K cascade:FGFR3 / STAT5 activation downstream of FLT3 ITD mutants / PI-3K cascade:FGFR2 / PI-3K cascade:FGFR4 / PI-3K cascade:FGFR1 / endodermal cell differentiation / regulation of MAPK cascade / GRB2:SOS provides linkage to MAPK signaling for Integrins / RHOU GTPase cycle / PI3K events in ERBB2 signaling / Signaling by ALK fusions and activated point mutants / SOS-mediated signalling / Activated NTRK3 signals through RAS / RET signaling / Activated NTRK2 signals through RAS / insulin receptor substrate binding / PI3K Cascade / Interleukin-3, Interleukin-5 and GM-CSF signaling / SHC1 events in ERBB4 signaling / RHO GTPases Activate WASPs and WAVEs / Signalling to RAS / fibroblast growth factor receptor signaling pathway / GAB1 signalosome / SHC-related events triggered by IGF1R / Activated NTRK2 signals through FRS2 and FRS3 / Role of LAT2/NTAL/LAB on calcium mobilization / Signal attenuation / Interleukin receptor SHC signaling / SHC-mediated cascade:FGFR3 / MET activates RAS signaling / Schwann cell development / Signaling by PDGFRA transmembrane, juxtamembrane and kinase domain mutants / Signaling by PDGFRA extracellular domain mutants / SHC-mediated cascade:FGFR2 / SHC-mediated cascade:FGFR4 / Signaling by FGFR4 in disease / SHC-mediated cascade:FGFR1 / Erythropoietin activates RAS / signal transduction in response to DNA damage / FRS-mediated FGFR3 signaling / Signaling by CSF3 (G-CSF) / Signaling by FLT3 ITD and TKD mutants / FRS-mediated FGFR2 signaling / FRS-mediated FGFR4 signaling / Signaling by FGFR3 in disease / FRS-mediated FGFR1 signaling / Tie2 Signaling / Signaling by FGFR2 in disease / GRB2 events in EGFR signaling / insulin-like growth factor receptor binding / SHC1 events in EGFR signaling / myelination / EGFR Transactivation by Gastrin / Signaling by FLT3 fusion proteins / FLT3 Signaling / Signaling by FGFR1 in disease / GRB2 events in ERBB2 signaling / NCAM signaling for neurite out-growth / phosphotyrosine residue binding / ephrin receptor binding / SHC1 events in ERBB2 signaling / Integrin signaling / Downstream signal transduction / Insulin receptor signalling cascade / Constitutive Signaling by Overexpressed ERBB2 / negative regulation of angiogenesis / FCERI mediated Ca+2 mobilization / InlB-mediated entry of Listeria monocytogenes into host cell / insulin-like growth factor receptor signaling pathway / Signaling by phosphorylated juxtamembrane, extracellular and kinase domain KIT mutants / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / cellular response to ionizing radiation
Similarity search - Function
Phosphotyrosine interaction domain, Shc-like / SH2 adaptor protein C, SH2 domain / GRB2, N-terminal SH3 domain / GRB2, C-terminal SH3 domain / Grb2-like / Phosphotyrosine interaction domain (PTB/PID) / Phosphotyrosine interaction domain (PID) profile. / Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain / PTB/PI domain / SH2 domain ...Phosphotyrosine interaction domain, Shc-like / SH2 adaptor protein C, SH2 domain / GRB2, N-terminal SH3 domain / GRB2, C-terminal SH3 domain / Grb2-like / Phosphotyrosine interaction domain (PTB/PID) / Phosphotyrosine interaction domain (PID) profile. / Phosphotyrosine-binding domain, phosphotyrosine-interaction (PI) domain / PTB/PI 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 / PH-like domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
SHC-transforming protein 1 / Growth factor receptor-bound protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR
AuthorsOgura, K.
CitationJournal: J.Mol.Biol. / Year: 1999
Title: Solution structure of the SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide.
Authors: Ogura, K. / Tsuchiya, S. / Terasawa, H. / Yuzawa, S. / Hatanaka, H. / Mandiyan, V. / Schlessinger, J. / Inagaki, F.
History
DepositionApr 19, 1999Deposition site: PDBE / Processing site: RCSB
Revision 1.0Apr 27, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details
Revision 1.4Dec 27, 2023Group: 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
E: PROTEIN (GROWTH FACTOR RECEPTOR BINDING PROTEIN)
I: PROTEIN (SHC-DERIVED PEPTIDE)


Theoretical massNumber of molelcules
Total (without water)13,6002
Polymers13,6002
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)1 / 100LOWEST ENERGY
Representative

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Components

#1: Protein PROTEIN (GROWTH FACTOR RECEPTOR BINDING PROTEIN) / GRB2-SH2


Mass: 12012.516 Da / Num. of mol.: 1 / Fragment: SH2
Source method: isolated from a genetically manipulated source
Details: RESIDUES HIS-58 - THR-159 AND THE EXTRINSIC N-TERMINAL TWO RESIDUES, GLY-56 AND SER-57
Source: (gene. exp.) Homo sapiens (human) / Plasmid: BL21 (DE3)
Gene (production host): PROTEIN WAS EXPRESSED WITH PGEX-4T-2 VECTOR AND BL21 (DE3) CELL AS GST-FUSION PROTEIN, AND CLEAVED WITH TRYPSIN
Production host: Escherichia coli (E. coli) / References: UniProt: P62993
#2: Protein/peptide PROTEIN (SHC-DERIVED PEPTIDE)


Mass: 1587.558 Da / Num. of mol.: 1 / Fragment: 423-435 / Source method: obtained synthetically
Details: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED BY THE SOLID-PHASE FMOC STRATEGY. THE SEQUENCE OF THIS PEPTIDE IS NATURALLY FOUND IN HOMO SAPIENS (HUMAN).
References: UniProt: P29353

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: MEAN STRUCTURE. NULL

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Sample preparation

Sample conditionspH: 6.3 / Temperature: 301 K
Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLORstructure solution
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 1

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