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@ARTICLE{Koruza:872857,
      author       = {Koruza, Katarina and Mahon, Brian P. and Blakeley, Matthew
                      P. and Ostermann, Andreas and Schrader, Tobias E. and
                      McKenna, Robert and Knecht, Wolfgang and Fisher, S. Zoë},
      title        = {{U}sing neutron crystallography to elucidate the basis of
                      selective inhibition of carbonic anhydrase by saccharin and
                      a derivative},
      journal      = {Journal of structural biology},
      volume       = {205},
      number       = {2},
      issn         = {1047-8477},
      address      = {San Diego, Calif.},
      publisher    = {Elsevier},
      reportid     = {FZJ-2020-00325},
      pages        = {147 - 154},
      year         = {2019},
      abstract     = {Up-regulation of carbonic anhydrase IX (CA IX) expression
                      is an indicator of metastasis and associated with poorcancer
                      patient prognosis. CA IX has emerged as a cancer drug target
                      but development of isoform-specific inhibitorsis challenging
                      due to other highly conserved CA isoforms. In this study, a
                      CA IXmimic construct was used(CA II with seven point
                      mutations introduced, to mimic CA IX active site) while
                      maintaining CA II solubility thatmake it amenable to
                      crystallography. The structures of CA IXmimic unbound and in
                      complex with saccharin (SAC)and a saccharin-glucose
                      conjugate (SGC) were determined using joint X-ray and
                      neutron protein crystallography.Previously, SAC and SGC have
                      been shown to display CA isoform inhibitor selectivity in
                      assays and X-ray crystalstructures failed to reveal the
                      basis of this selectivity. Joint X-ray and neutron
                      crystallographic studies haveshown active site residues,
                      solvent, and H-bonding re-organization upon SAC and SGC
                      binding. These observationshighlighted the importance of
                      residues 67 (Asn in CA II, Gln in CA IX) and 130 (Asp in CA
                      II, Arg in CAIX) in selective CA inhibitor targeting.},
      cin          = {JCNS-FRM-II / JCNS-1 / MLZ},
      ddc          = {540},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106 / I:(DE-588b)4597118-3},
      pnm          = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6G15 - FRM II / MLZ (POF3-6G15) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30639924},
      UT           = {WOS:000460494000004},
      doi          = {10.1016/j.jsb.2018.12.009},
      url          = {https://juser.fz-juelich.de/record/872857},
}