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Title: Crystal Structures of Cisplatin Bound to a Human Copper Chaperone

Journal Article · · J. Am. Chem. Soc.
DOI:https://doi.org/10.1021/ja906363t· OSTI ID:1006126

Copper trafficking proteins, including the chaperone Atox1 and the P{sub 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.

Research Organization:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Organization:
USDOE
OSTI ID:
1006126
Journal Information:
J. Am. Chem. Soc., Vol. 131, Issue (40) ; 10, 2009; ISSN 0002-7863
Country of Publication:
United States
Language:
ENGLISH

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