Replacement of lys 622 in the ATP binding domain of P100gag-mil abolishes the in vitro autophosphorylation of the protein and the biological properties of the v-mil oncogene of MH2 virus.

@article{Denhez1988ReplacementOL,
  title={Replacement of lys 622 in the ATP binding domain of P100gag-mil abolishes the in vitro autophosphorylation of the protein and the biological properties of the v-mil oncogene of MH2 virus.},
  author={F Denhez and Barbara Heimann and L. d'Auriol and Thomas Graf and M Coquillaud and Jean Coll and Francis Galibert and Karin Moelling and Dominique St{\'e}helin and Jacques Ghysdael},
  journal={The EMBO journal},
  year={1988},
  volume={7 2},
  pages={541-6}
}
Lysine 622 in the ATP-binding domain of P100gag-mil, the translation product of the v-mil oncogene of MH2, has been replaced with methionine using oligonucleotide site-directed mutagenesis. This substitution results in the inactivation of the serine/threonine-specific autophosphorylation of P100gag-mil in vitro, indicating that this activity is an intrinsic property of the viral protein. This substitution also suppresses two of the biological properties of MH2 which have previously been shown… CONTINUE READING

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