1FU6

NMR STRUCTURE OF THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3-KINASE


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 110 
  • Conformers Submitted: 
  • Selection Criteria: structures with favorable non-bond energy 

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This is version 1.3 of the entry. See complete history


Literature

NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site.

Weber, T.Schaffhausen, B.Liu, Y.Gunther, U.L.

(2000) Biochemistry 39: 15860-15869

  • DOI: https://doi.org/10.1021/bi001474d
  • Primary Citation of Related Structures:  
    1FU5, 1FU6

  • PubMed Abstract: 

    The N-terminal src homology 2 (SH2) domain of the p85 subunit of phosphoinositide 3-kinase (PI3K) has a higher affinity for a peptide with two phosphotyrosines than for the same peptide with only one. This unexpected result was not observed for the C-terminal SH2 from the same protein. NMR structural analysis has been used to understand the behavior of the N-SH2. The structure of the free SH2 domain has been compared to that of the SH2 complexed with a doubly phosphorylated peptide derived from polyomavirus middle T antigen (MT). The structure of the free SH2 domain shows some differences from previous NMR and X-ray structures. In the N-SH2 complexed with a doubly phosphorylated peptide, a second site for phosphotyrosine interaction has been identified. Further, line shapes of NMR signals showed that the SH2 protein-ligand complex is subject to temperature-dependent conformational mobility. Conformational mobility is also supported by the spectra of the ligand peptide. A binding model which accounts for these results is developed.


  • Organizational Affiliation

    Institut für Biophysikalische Chemie, J. W. Goethe Universität, Frankfurt, Biozentrum N230, Marie-Curie-Strasse 9, 60439 Frankfurt, Germany.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY ALPHA SUBUNIT111Rattus norvegicusMutation(s): 0 
UniProt
Find proteins for Q63787 (Rattus norvegicus)
Explore Q63787 
Go to UniProtKB:  Q63787
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ63787
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 110 
  • Conformers Submitted: 
  • Selection Criteria: structures with favorable non-bond energy 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-02-21
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-23
    Changes: Data collection, Database references, Derived calculations