Crystal structures of cisplatin bound to a human copper chaperone

J Am Chem Soc. 2009 Oct 14;131(40):14196-7. doi: 10.1021/ja906363t.


Copper trafficking proteins, including the chaperone Atox1 and the P(1B)-type ATPase ATP7B, have been implicated in cellular resistance to the anticancer drug cisplatin. We have determined two crystal structures of cisplatin-Atox1 adducts that reveal platinum coordination by the conserved CXXC copper-binding motif. Direct interaction of cisplatin with this functionally relevant site has significant implications for understanding the molecular basis for resistance mediated by copper transport pathways.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Binding Sites
  • Cation Transport Proteins / chemistry*
  • Cisplatin / chemistry*
  • Copper / chemistry*
  • Crystallography, X-Ray
  • Humans
  • Metallochaperones
  • Models, Molecular
  • Molecular Chaperones / chemistry*


  • ATOX1 protein, human
  • Cation Transport Proteins
  • Metallochaperones
  • Molecular Chaperones
  • Copper
  • Cisplatin