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@ARTICLE{Calandrini:201315,
      author       = {Calandrini, Vania and Arnesano, Fabio and Galliani, Angela
                      and Nguyen, Trung Hai and Ippoliti, Emiliano and Carloni,
                      Paolo and Natile, Giovanni},
      title        = {{P}latination of the copper transporter {ATP}7{A} involved
                      in anticancer drug resistance},
      journal      = {Dalton transactions},
      volume       = {43},
      number       = {31},
      issn         = {1477-9234},
      address      = {London},
      publisher    = {Soc.},
      reportid     = {FZJ-2015-03620},
      pages        = {12085 -},
      year         = {2014},
      abstract     = {The clinical efficacy of the widely used anticancer drug
                      cisplatin is severely limited by the emergence of
                      resistance. This is related to the drug binding to proteins
                      such as the copper influx transporter Ctr1, the copper
                      chaperone Atox1, and the copper pumps ATP7A and ATP7B. While
                      the binding modes of cisplatin to the first two proteins are
                      known, the structural determinants of platinated ATP7A/ATP7B
                      are lacking. Here we investigate the interaction of
                      cisplatin with the first soluble domain of ATP7A. First, we
                      establish by ESI-MS and 1H, 13C, and 15N NMR that, in
                      solution, the adduct is a monomer in which the sulfur atoms
                      of residues Cys19 and Cys22 are cis-coordinated to the
                      [Pt(NH3)2]2+ moiety. Then, we carry out hybrid
                      Car–Parrinello QM/MM simulations and computational
                      spectroscopy calculations on a model adduct based on the NMR
                      structure of the apo protein and featuring the
                      experimentally determined binding mode of the metal ion.
                      These calculations show quantitative agreement with CD
                      spectra and 1H, 13C, and 15N NMR chemical shifts, thus
                      providing a quantitative molecular view of the 3D binding
                      mode of cisplatin to ATP7A. Importantly, the same comparison
                      rules out a variety of alternative models with different
                      coordination modes, that we explored to test the robustness
                      of the computational approach. Using this combined in
                      silico–in vitro approach we provide here for the first
                      time a quantitative 3D atomic view of the platinum binding
                      to the first soluble domain of ATP7A.},
      cin          = {INM-9 / IAS-5 / GRS},
      ddc          = {540},
      cid          = {I:(DE-Juel1)INM-9-20140121 / I:(DE-Juel1)IAS-5-20120330 /
                      I:(DE-Juel1)GRS-20100316},
      pnm          = {899 - ohne Topic (POF2-899)},
      pid          = {G:(DE-HGF)POF2-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000339862400036},
      pubmed       = {pmid:24983998},
      doi          = {10.1039/C4DT01339E},
      url          = {https://juser.fz-juelich.de/record/201315},
}