Cisplatin binds human copper chaperone Atox1 and promotes unfolding in vitro.

  title={Cisplatin binds human copper chaperone Atox1 and promotes unfolding in vitro.},
  author={Maria E Palm and Christoph F. Weise and Christina Lundin and Gunnar Wingsle and Yvonne Nygren and Erik Bj{\"o}rn and Peter Naredi and Magnus Wolf-Watz and Pernilla Wittung-Stafshede},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={108 17},
Cisplatin (cisPt), Pt(NH(3))(2)Cl(2), is a cancer drug believed to kill cells via DNA binding and damage. Recent work has implied that the cellular copper (Cu) transport machinery may be involved in cisPt cell export and drug resistance. Normally, the Cu chaperone Atox1 binds Cu(I) via two cysteines and delivers the metal to metal-binding domains of ATP7B; the ATP7B domains then transfer the metal to the Golgi lumen for loading on cuproenzymes. Here, we use spectroscopic methods to test if… CONTINUE READING

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