Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation.

  title={Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation.},
  author={Jing Yang and Peter D. Cron and Vivienne Thompson and Valerie M. Good and Daniel Hess and Brian A. Hemmings and David Barford},
  journal={Molecular cell},
  volume={9 6},
Protein kinase B/Akt plays crucial roles in promoting cell survival and mediating insulin responses. The enzyme is stimulated by phosphorylation at two regulatory sites: Thr 309 of the activation segment and Ser 474 of the hydrophobic motif, a conserved feature of many AGC kinases. Analysis of the crystal structures of the unphosphorylated and Thr 309 phosphorylated states of the PKB kinase domain provides a molecular explanation for regulation by Ser 474 phosphorylation. Activation by Ser 474… CONTINUE READING
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