Crystal structures of cisplatin bound to a human copper chaperone

Amie K. Boal; Amy C. Rosenzweig

doi:10.1021/ja906363t

Crystal structures of cisplatin bound to a human copper chaperone

Amie K. Boal, Amy C. Rosenzweig

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141 Scopus citations

Abstract

(Chemical Equation Presented). 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.

Original language	English (US)
Pages (from-to)	14196-14197
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	131
Issue number	40
DOIs	https://doi.org/10.1021/ja906363t
State	Published - Oct 14 2009

All Science Journal Classification (ASJC) codes

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja906363t

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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.",

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AB - (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.

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Crystal structures of cisplatin bound to a human copper chaperone

Abstract

All Science Journal Classification (ASJC) codes

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