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@ARTICLE{Werner:646219,
      author       = {Werner, Christian and Barthel, Tatjana and Harasimowicz,
                      Hugo and Marminon, Christelle and Weiss, Manfred S. and
                      Borgne, Marc Le and Niefind, Karsten},
      title        = {{C}rystallographic {F}ragment {S}creening with {CK}2α’,
                      an {I}soform of {H}uman {P}rotein {K}inase {CK}2 {C}atalytic
                      {S}ubunit, and {I}ts {U}se to {O}btain a
                      {CK}2α’/{H}eparin {C}omplex {S}tructure},
      journal      = {Kinases and Phosphatases},
      volume       = {4},
      number       = {1},
      issn         = {2813-3757},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {PUBDB-2026-00764},
      pages        = {1 -},
      year         = {2026},
      abstract     = {CK2α and CK2α’, two paralogous members of the human
                      kinome, are catalytic subunits of protein kinase CK2.
                      Together with the regulatory subunit CK2β, they form
                      heterotetrameric holoenzymes. CK2 is the subject of efforts
                      to develop effective and selective inhibitors. For this,
                      secondary binding sites remote from the canonical ATP/GTP
                      cavity are critical. A crystallographic fragment screening
                      with CK2α’ crystals and an established molecular fragment
                      collection was performed to identify new ligands at known or
                      novel sites. It resulted in fourteen CK2α’/fragment
                      structures. Five fragments were found at the CK2β interface
                      of CK2α’ and three fragments at the established αD
                      pocket, which exhibits subtle differences between CK2α and
                      CK2α’; comparative co-crystallisations with CK2α showed
                      that one of them binds to the αD pocket of CK2α’
                      exclusively. No fragments bound at the substrate-binding
                      region of CK2α’, but a CK2α’ structure with dp10, a
                      decameric section of the substrate-competitive inhibitor
                      heparin, and the indenoindole-type ATP-competitive inhibitor
                      4w was determined. A comparison with a published CK2α/dp10
                      structure revealed features consistent with reports about
                      substrate specificity differences between the isoenzymes:
                      dp10 binds to CK2α’ and CK2α with opposite strand
                      orientations, and the local conformations of the isoenzymes
                      in the helix αD region are significantly different.},
      cin          = {EMBL-User},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.3390/kinasesphosphatases4010001},
      url          = {https://bib-pubdb1.desy.de/record/646219},
}