Both ATP sites of human P-glycoprotein are essential but not symmetric.

@article{Hrycyna1999BothAS,
  title={Both ATP sites of human P-glycoprotein are essential but not symmetric.},
  author={Christine A Hrycyna and M. Ramachandra and Ursula A. Germann and P. W. Cheng and Ira Pastan and Michael M. Gottesman},
  journal={Biochemistry},
  year={1999},
  volume={38 42},
  pages={13887-99}
}
Human P-glycoprotein (P-gp) is a cell surface drug efflux pump that contains two nucleotide binding domains (NBDs). Mutations were made in each of the Walker B consensus motifs of the NBDs at positions D555N and D1200N, thought to be involved in Mg(2+) binding. Although the mutant and wild-type P-gps were expressed equivalently at the cell surface and bound the drug analogue [(125)I]iodoarylazidoprazosin ([(125)I]IAAP) comparably, neither of the mutant proteins was able to transport fluorescent… CONTINUE READING

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Multidrug Resistance in Cancer Cells(Gupta, S., and Tsuruo, T., Eds.) pp 29 -37

  • C. A. Hrycyna, S. Zhang, M. Ramachandra, B. Ni, I. Pastan, M. M. Gottesman
  • 1996

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