Detail The Structure of a Human p110/p85 Complex Elucidates the Effects of Oncogenic PI3K Mutations   Oleh:  Chuan-Hsiang, Huang ; Mandelker, Diana ; Schmidt-Kittler, Oleg ; Samuels, Yardena ; Velculescu, Victor E. ; Kinzler, Kenneth W. ; Vogelstein, Bert ; Gabelli, Sandra B. ; Amzel, L. Mario Jenis: Article from Bulletin/Magazine Dalam koleksi: SCIENCE (keterangan: ada di Proquest) vol. 318 no. 5867 (Dec. 2007), page 1744. Ketersediaan Perpustakaan FK Nomor Panggil: S01.K.2007.09 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada     Lihat Detail Induk Isi artikel PIK3CA, one of the two most frequently mutated oncogenes in human tumors, codes for p110, the catalytic subunit of a phosphatidylinositol 3-kinase, isoform (PI3K, p110/p85). Here, we report a 3.0 angstrom resolution structure of a complex between p110 and a polypeptide containing the p110-binding domains of p85, a protein required for its enzymatic activity. The structure shows that many of the mutations occur at residues lying at the interfaces between p110 and p85 or between the kinase domain of p110 and other domains within the catalytic subunit. Disruptions of these interactions are likely to affect the regulation of kinase activity by p85 or the catalytic activity of the enzyme, respectively. In addition to providing new insights about the structure of PI3K, these results suggest specific mechanisms for the effect of oncogenic mutations in p110 and p85. Opini Anda Klik untuk menuliskan opini Anda tentang koleksi ini! Kembali

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