Activation of the Sire-family tyrosine kinase Hck by SH3 domain displacement

@article{Moarefi1997ActivationOT,
  title={Activation of the Sire-family tyrosine kinase Hck by SH3 domain displacement},
  author={Ismail Moarefi and Michelle LaFevre-Bernt and Frank Sicheri and Morgan Huse and C Lee and John Kuriyan and W Todd Miller},
  journal={Nature},
  year={1997},
  volume={385},
  pages={650-653}
}
The protein Hck is a member of the Src family of non-receptor tyrosine kinases which is preferentially expressed in haematopoietic cells of the myeloid and B-lymphoid lineages1,2. Src kinases are inhibited by tyrosine-phosphorylation at a carboxy-terminal site3–9. The SH2 domains of these enzymes play an essential role in this regulation by binding to the tyrosine-phosphorylated tail8–11. The crystal structure of the downregulated form of Hck has been determined12 and reveals that the SH2… CONTINUE READING
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