3IWL

Crystal structure of cisplatin bound to a human copper chaperone (monomer)

Summary for 3IWL

Entry DOI	10.2210/pdb3iwl/pdb
Related	3IWX
Descriptor	Copper transport protein ATOX1, PLATINUM (II) ION, SULFATE ION, ... (5 entities in total)
Functional Keywords	beta-alpha-beta-beta-alpha-beta, transport protein, cisplatin, platinum, chaperone, copper, copper transport, ion transport, metal-binding, transport, metal transport
Biological source	Homo sapiens (human)
Total number of polymer chains	1
Total formula weight	7953.97
Authors	Boal, A.K.,Rosenzweig, A.C. (deposition date: 2009-09-02, release date: 2009-09-22, Last modification date: 2024-02-21)
Primary citation	Boal, A.K.,Rosenzweig, A.C. Crystal structures of cisplatin bound to a human copper chaperone. J.Am.Chem.Soc., 131:14196-14197, 2009 Cited by PubMed 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. PubMed: 19807176 DOI: 10.1021/ja906363t PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.6 Å)

Structure validation