Structural highlights
Function
[ATOX1_HUMAN] Binds and deliver cytosolic copper to the copper ATPase proteins. May be important in cellular antioxidant defense.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structures of cisplatin bound to a human copper chaperone.,Boal AK, Rosenzweig AC J Am Chem Soc. 2009 Oct 14;131(40):14196-7. PMID:19807176[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Boal AK, Rosenzweig AC. Crystal structures of cisplatin bound to a human copper chaperone. J Am Chem Soc. 2009 Oct 14;131(40):14196-7. PMID:19807176 doi:10.1021/ja906363t
