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@ARTICLE{Schiebel:859974,
      author       = {Schiebel, Johannes and Gaspari, Roberto and Wulsdorf,
                      Tobias and Ngo, Khang and Sohn, Christian and Schrader,
                      Tobias E. and Cavalli, Andrea and Ostermann, Andreas and
                      Heine, Andreas and Klebe, Gerhard},
      title        = {{I}ntriguing role of water in protein-ligand binding
                      studied by neutron crystallography on trypsin complexes},
      journal      = {Nature Communications},
      volume       = {9},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {FZJ-2019-00780},
      pages        = {3559},
      year         = {2018},
      abstract     = {Hydrogen bonds are key interactions determining
                      protein-ligand binding affinity and therefore fundamental to
                      any biological process. Unfortunately, explicit structural
                      information about hydrogen positions and thus H-bonds in
                      protein-ligand complexes is extremely rare and similarly the
                      important role of water during binding remains poorly
                      understood. Here, we report on neutron structures of trypsin
                      determined at very high resolutions ≤1.5 Å in
                      uncomplexed and inhibited state complemented by X-ray and
                      thermodynamic data and computer simulations. Our structures
                      show the precise geometry of H-bonds between protein and the
                      inhibitors N-amidinopiperidine and benzamidine along with
                      the dynamics of the residual solvation pattern. Prior to
                      binding, the ligand-free binding pocket is occupied by water
                      molecules characterized by a paucity of H-bonds and high
                      mobility resulting in an imperfect hydration of the critical
                      residue Asp189. This phenomenon likely constitutes a key
                      factor fueling ligand binding via water displacement and
                      helps improving our current view on water influencing
                      protein–ligand recognition.},
      cin          = {JCNS-FRM-II / Neutronenstreuung ; JCNS-1},
      ddc          = {500},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218 /
                      I:(DE-Juel1)JCNS-1-20110106},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623) / 6215 - Soft Matter,
                      Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215},
      experiment   = {EXP:(DE-MLZ)BIODIFF-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30177695},
      UT           = {WOS:000443465900001},
      doi          = {10.1038/s41467-018-05769-2},
      url          = {https://juser.fz-juelich.de/record/859974},
}