Domain mapping of the photoaffinity drug-binding sites in P-glycoprotein encoded by mouse mdr1b.

@article{Greenberger1991DomainMO,
  title={Domain mapping of the photoaffinity drug-binding sites in P-glycoprotein encoded by mouse mdr1b.},
  author={Lee M. Greenberger and Christopher J. Lisanti and Jersone Tasso Moreira Silva and Susan Band Horwitz},
  journal={The Journal of biological chemistry},
  year={1991},
  volume={266 31},
  pages={20744-51}
}
P-glycoprotein is an energy-dependent drug efflux pump with broad specificity for hydrophobic antitumor agents such as vinblastine, doxorubicin, and taxol. We have previously shown that [3H]azidopine and [125I] iodoaryl azidoprazosin, which are photoaffinity probes for the alpha 1-subunit of the L-type calcium channel and alpha 1-adrenergic receptor, respectively, specifically interact with P-glycoprotein, partially reverse multidrug resistance, and bind to a 6-kDa common domain in the 140-kDa… CONTINUE READING
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