The rapamycin-binding domain governs substrate selectivity by the mammalian target of rapamycin.

@article{McMahon2002TheRD,
  title={The rapamycin-binding domain governs substrate selectivity by the mammalian target of rapamycin.},
  author={Lloyd P McMahon and Kin Man Choi and Tai-an Lin and Robert T. Abraham and John C. Lawrence},
  journal={Molecular and cellular biology},
  year={2002},
  volume={22 21},
  pages={7428-38}
}
The mammalian target of rapamycin (mTOR) is a Ser/Thr (S/T) protein kinase, which controls mRNA translation initiation by modulating phosphorylation of the translational regulators PHAS-I and p70(S6K). Here we show that in vitro mTOR is able to phosphorylate these two regulators at comparable rates. Both (S/T)P sites, such as Thr36, Thr45, and Thr69 in PHAS-I and the h(S/T)h site (where h is a hydrophobic amino acid) Thr389 in p70(S6K), were phosphorylated. Rapamycin-FKBP12 inhibited mTOR… CONTINUE READING

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