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

Crystal structures of cisplatin bound to a human copper chaperone.

Author information

1
Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.

Abstract

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.

PMID:
19807176
PMCID:
PMC2760026
DOI:
10.1021/ja906363t
[Indexed for MEDLINE]
Free PMC Article

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