Crystal structures of cisplatin bound to a human copper chaperone

Amie Kathleen Boal, Amy C. Rosenzweig

Research output: Contribution to journalArticle

113 Citations (Scopus)

Abstract

(Chemical Equation Presented). Copper trafficking proteins, including the chaperone Atox1 and the P1B-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.

Original languageEnglish (US)
Pages (from-to)14196-14197
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number40
DOIs
StatePublished - Oct 14 2009

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Cisplatin
Copper
Crystal structure
Protein Transport
Platinum
Adenosine Triphosphatases
Proteins
Pharmaceutical Preparations

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

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Crystal structures of cisplatin bound to a human copper chaperone. / Boal, Amie Kathleen; Rosenzweig, Amy C.

In: Journal of the American Chemical Society, Vol. 131, No. 40, 14.10.2009, p. 14196-14197.

Research output: Contribution to journalArticle

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