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@ARTICLE{Mehlman:612788,
      author       = {Mehlman, Tamar and Ginn, Helen M. and Keedy, Daniel A.},
      title        = {{A}n expanded trove of fragment-bound structures for the
                      allosteric enzyme {PTP}1{B} from computational reanalysis of
                      large-scale crystallographic data},
      journal      = {Structure},
      volume       = {32},
      number       = {8},
      issn         = {0969-2126},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {PUBDB-2024-05462},
      pages        = {1231 - 1238.e4},
      year         = {2024},
      note         = {Waiting for fulltext},
      abstract     = {Due to their low binding affinities, detecting
                      small-molecule fragments bound to protein structures from
                      crystallographic datasets has been a challenge. Here, we
                      report a trove of 65 new fragment hits for PTP1B, an
                      “undruggable” therapeutic target enzyme for diabetes and
                      cancer. These structures were obtained from computational
                      analysis of data from a large crystallographic screen,
                      demonstrating the power of this approach to elucidate many
                      $(∼50\%$ more) “hidden” ligand-bound states of
                      proteins. Our new structures include a fragment hit found in
                      a novel binding site in PTP1B with a unique location
                      relative to the active site, one that links adjacent
                      allosteric sites, and, perhaps most strikingly, a fragment
                      that induces long-range allosteric protein conformational
                      responses. Altogether, our research highlights the utility
                      of computational analysis of crystallographic data, makes
                      publicly available dozens of new ligand-bound structures of
                      a high-value drug target, and identifies novel aspects of
                      ligandability and allostery in PTP1B.},
      cin          = {FS-CFEL-1-DNMX},
      ddc          = {540},
      cid          = {I:(DE-H253)FS-CFEL-1-DNMX-20231108},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / VH-NG-19-02 - Working with RoPE:
                      Representation of Protein Entities $(2023_IVF-VH-NG-19-02)$
                      / DFG project G:(GEPRIS)390715994 - EXC 2056: CUI: Tiefe
                      Einblicke in Materie (390715994)},
      pid          = {G:(DE-HGF)POF4-633 / $G:(DE-HGF)2023_IVF-VH-NG-19-02$ /
                      G:(GEPRIS)390715994},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38861991},
      UT           = {WOS:001292191500001},
      doi          = {10.1016/j.str.2024.05.010},
      url          = {https://bib-pubdb1.desy.de/record/612788},
}