The Structure of a Human p110α/p85α Complex Elucidates the Effects of Oncogenic PI3Kα Mutations

@article{Huang2007TheSO,
  title={The Structure of a Human p110$\alpha$/p85$\alpha$ Complex Elucidates the Effects of Oncogenic PI3K$\alpha$ Mutations},
  author={Chuangfang Huang and D. Mandelker and O. Schmidt-Kittler and Y. Samuels and V. Velculescu and K. Kinzler and B. Vogelstein and S. Gabelli and L. Amzel},
  journal={Science},
  year={2007},
  volume={318},
  pages={1744 - 1748}
}
PIK3CA, one of the two most frequently mutated oncogenes in human tumors, codes for p110α, the catalytic subunit of a phosphatidylinositol 3-kinase, isoform α (PI3Kα, p110α/p85). Here, we report a 3.0 angstrom resolution structure of a complex between p110α and a polypeptide containing the p110α-binding domains of p85α, a protein required for its enzymatic activity. The structure shows that many of the mutations occur at residues lying at the interfaces between p110α and p85α or between the… Expand
A frequent kinase domain mutation that changes the interaction between PI3Kα and the membrane
Class I PI3K in oncogenic cellular transformation
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