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@ARTICLE{LaSala:1008583,
      author       = {La Sala, Giuseppina and Pfleger, Christopher and Käck,
                      Helena and Wissler, Lisa and Nevin, Philip and Böhm,
                      Kerstin and Janet, Jon Paul and Schimpl, Marianne and
                      Stubbs, Christopher J. and De Vivo, Marco and Tyrchan,
                      Christian and Hogner, Anders and Gohlke, Holger and Frolov,
                      Andrey I.},
      title        = {{C}ombining structural and coevolution information to
                      unveil allosteric sites},
      journal      = {Chemical science},
      volume       = {14},
      number       = {25},
      issn         = {2041-6520},
      address      = {Cambridge},
      publisher    = {RSC},
      reportid     = {FZJ-2023-02416},
      pages        = {7057-7067},
      year         = {2023},
      note         = {This is an open access publication.},
      abstract     = {Understanding allosteric regulation in biomolecules is of
                      great interest to pharmaceutical research and computational
                      methods emerged during the last decades to characterize
                      allosteric coupling. However, the prediction of allosteric
                      sites in a protein structure remains a challenging task.
                      Here, we integrate local binding site information,
                      coevolutionary information, and information on dynamic
                      allostery into a structure-based three-parameter model to
                      identify potentially hidden allosteric sites in ensembles of
                      protein structures with orthosteric ligands. When tested on
                      five allosteric proteins (LFA-1, p38-α, GR, MAT2A, and
                      BCKDK), the model successfully ranked all known allosteric
                      pockets in the top three positions. Finally, we identified a
                      novel druggable site in MAT2A confirmed by X-ray
                      crystallography and SPR and a hitherto unknown druggable
                      allosteric site in BCKDK validated by biochemical and X-ray
                      crystallography analyses. Our model can be applied in drug
                      discovery to identify allosteric pockets.},
      cin          = {NIC / JSC / IBI-7 / IBG-4},
      ddc          = {540},
      cid          = {I:(DE-Juel1)NIC-20090406 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)IBI-7-20200312 / I:(DE-Juel1)IBG-4-20200403},
      pnm          = {5111 - Domain-Specific Simulation $\&$ Data Life Cycle Labs
                      (SDLs) and Research Groups (POF4-511) / 2171 - Biological
                      and environmental resources for sustainable use (POF4-217) /
                      Forschergruppe Gohlke $(hkf7_20200501)$},
      pid          = {G:(DE-HGF)POF4-5111 / G:(DE-HGF)POF4-2171 /
                      $G:(DE-Juel1)hkf7_20200501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37389247},
      UT           = {WOS:001004486700001},
      doi          = {10.1039/D2SC06272K},
      url          = {https://juser.fz-juelich.de/record/1008583},
}