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@ARTICLE{WiniewskaSzajewska:491472,
      author       = {Winiewska-Szajewska, Maria and Czapinska, Honorata and
                      Kaus-Drobek, Magdalena and Fricke, Anna and Mieczkowska,
                      Kinga and Dadlez, Michał and Bochtler, Matthias and
                      Poznański, Jarosław},
      title        = {{C}ompetition between electrostatic interactions and
                      halogen bonding in the protein–ligand system: structural
                      and thermodynamic studies of
                      5,6-dibromobenzotriazole-h{CK}2$α$ complexes},
      journal      = {Scientific reports},
      volume       = {12},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {PUBDB-2023-00181},
      pages        = {18964},
      year         = {2022},
      abstract     = {CK2 is a member of the CMGC group of eukaryotic protein
                      kinases and a cancer drug target. It can be efficiently
                      inhibited by halogenated benzotriazoles and benzimidazoles.
                      Depending on the scaffold, substitution pattern, and pH,
                      these compounds are either neutral or anionic. Their binding
                      poses are dictated by a hydrophobic effect (desolvation) and
                      a tug of war between a salt bridge/hydrogen bond (to K68)
                      and halogen bonding (to E114 and V116 backbone oxygens).
                      Here, we test the idea that binding poses might be
                      controllable by pH for ligands with near-neutral pK$_a$,
                      using the conditionally anionic 5,6-DBBt and constitutively
                      anionic TBBt as our models. We characterize the binding by
                      low-volume Differential Scanning Fluorimetry (nanoDSF),
                      Isothermal Calorimetry (ITC), Hydrogen/Deuterium eXchange
                      (HDX), and X-ray crystallography (MX). The data indicate
                      that the ligand pose away from the hinge dominates for the
                      entire tested pH range (5.5–8.5). The insensitivity of the
                      binding mode to pH is attributed to the perturbation of
                      ligand pK$_a$ upon binding that keeps it anionic in the
                      ligand binding pocket at all tested pH values. However, a
                      minor population of the ligand, detectable only by HDX,
                      shifts towards the hinge in acidic conditions. Our findings
                      demonstrate that electrostatic (ionic) interactions
                      predominate over halogen bonding.},
      cin          = {DOOR ; HAS-User / EMBL},
      ddc          = {600},
      cid          = {I:(DE-H253)HAS-User-20120731 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / BIOSTRUCT-X -
                      Transnational access and enhancement of integrated
                      Biological Structure determination at synchrotron X-ray
                      radiation facilities (283570)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(EU-Grant)283570},
      experiment   = {EXP:(DE-H253)P-P11-20150101 / EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {36347916},
      UT           = {WOS:000880437400063},
      doi          = {10.1038/s41598-022-23611-0},
      url          = {https://bib-pubdb1.desy.de/record/491472},
}