Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.14
Classification:METAL TRANSPORT
Release Date:2009-09-22
Deposition Date:2009-09-03
Revision Date:2011-07-13
Molecular Weight:15413.53
Macromolecule Type:Protein
Residue Count:136
Atom Site Count:1029
DOI:10.2210/pdb3iwx/pdb
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.
Resolution:2.14
Classification:METAL TRANSPORT
Release Date:2009-09-22
Deposition Date:2009-09-03
Revision Date:2011-07-13
Molecular Weight:15413.53
Macromolecule Type:Protein
Residue Count:136
Atom Site Count:1029
DOI:10.2210/pdb3iwx/pdb
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.
| Date made available | 2009 |
|---|---|
| Publisher | RCSB-PDB |