1QG1

GROWTH FACTOR RECEPTOR BINDING PROTEIN SH2 DOMAIN COMPLEXED WITH AN SHC-DERIVED PEPTIDE


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 
  • Selection Criteria: LOWEST ENERGY 

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This is version 1.4 of the entry. See complete history


Literature

Solution structure of the SH2 domain of Grb2 complexed with the Shc-derived phosphotyrosine-containing peptide.

Ogura, K.Tsuchiya, S.Terasawa, H.Yuzawa, S.Hatanaka, H.Mandiyan, V.Schlessinger, J.Inagaki, F.

(1999) J Mol Biol 289: 439-445

  • DOI: https://doi.org/10.1006/jmbi.1999.2792
  • Primary Citation of Related Structures:  
    1QG1

  • PubMed Abstract: 

    The solution structure of growth factor receptor-bound protein 2 (Grb2) SH2 complexed with a Shc-derived phosphotyrosine (pTyr)-containing peptide was determined by nuclear magnetic resonance (NMR) spectroscopy. The pTyr binding site of Grb2 SH2 was similar to those of other SH2 domains. In contrast, the amino acid residues C-terminal to pTyr did not form an extended structure because of steric hindrance caused by a bulky side-chain of Trp121 (EF1). As a result, the peptide formed a turn-structure on the surface of Grb2 SH2. The asparagine residue at the pTyr+2 position of the Shc-peptide interacted with the main-chain carbonyl groups of Lys109 and Leu120. The present solution structure was similar to the crystal structure reported for Grb2 SH2 complexed with a BCR-Abl-derived phosphotyrosine-containing peptide. Finally, the structure of Grb2 SH2 domain was compared with those of the complexes of Src and phospholipase C-gamma1 with their cognate peptides, showing that the specific conformation of the peptide was required for binding to the SH2 domains.


  • Organizational Affiliation

    Department of Molecular Physiology, Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome Bunkyo-ku, Tokyo, 113, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (GROWTH FACTOR RECEPTOR BINDING PROTEIN)A [auth E]104Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P62993 (Homo sapiens)
Explore P62993 
Go to UniProtKB:  P62993
PHAROS:  P62993
GTEx:  ENSG00000177885 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP62993
Sequence Annotations
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  • Reference Sequence

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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEIN (SHC-DERIVED PEPTIDE)B [auth I]13N/AMutation(s): 1 
UniProt & NIH Common Fund Data Resources
Find proteins for P29353 (Homo sapiens)
Explore P29353 
Go to UniProtKB:  P29353
PHAROS:  P29353
GTEx:  ENSG00000160691 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP29353
Sequence Annotations
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  • Reference Sequence
Small Molecules
Modified Residues  1 Unique
IDChains TypeFormula2D DiagramParent
PTR
Query on PTR
B [auth I]L-PEPTIDE LINKINGC9 H12 N O6 PTYR
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 
  • Selection Criteria: LOWEST ENERGY 

Structure Validation

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Entry History 

Deposition Data

  • Released Date: 1999-04-27 
  • Deposition Author(s): Ogura, K.

Revision History  (Full details and data files)

  • Version 1.0: 1999-04-27
    Type: Initial release
  • Version 1.1: 2008-04-26
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-03-02
    Changes: Database references, Derived calculations
  • Version 1.4: 2023-12-27
    Changes: Data collection