Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes

@article{Nolte1996CrystalSO,
  title={Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes},
  author={Robert T Nolte and Michael J. Eck and Joseph Schlessinger and Steven E. Shoelson and Stephen C Harrison},
  journal={Nature Structural Biology},
  year={1996},
  volume={3},
  pages={364-374}
}
Crystal structures of the amino-terminal SH2 domain of the p85α subunit of phosphatidylinositol (PI) 3-kinase, alone and in complex with phosphopeptides bearing pTyr-Met/Val-Xaa-Met motifs, show that phosphopeptides bind in the two-pronged manner seen in high-affinity Lck and Src SH2 complexes, with conserved interactions between the domain and the peptide segment from phosphotyrosine to Met+3. Peptide binding requires the rearrangement of a tyrosyl side chain in the BG loop to create the… CONTINUE READING

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