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@ARTICLE{Gabriel:615561,
      author       = {Gabriel, Florian and Spriestersbach, Lea and Fuhrmann,
                      Antonia and Jungnickel, Katharina E. J. and Mostafavi,
                      Siavash and Pardon, Els and Steyaert, Jan and Löw,
                      Christian},
      title        = {{S}tructural basis of thiamine transport and drug
                      recognition by {SLC}19{A}3},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2024-06168},
      pages        = {8542},
      year         = {2024},
      note         = {FG (grant numbers INST 152/772-1 | 152/774-1 | 152/775-1 |
                      152/776-1 | 152/777-1 FUGG},
      abstract     = {Thiamine (vitamin B1) functions as an essential coenzyme in
                      cells. Humans and other mammals cannot synthesise this
                      vitamin de novo and thus have to take it up from their diet.
                      Eventually, every cell needs to import thiamine across its
                      plasma membrane, which is mainly mediated by the two
                      specific thiamine transporters SLC19A2 and SLC19A3. Loss of
                      function mutations in either of these transporters lead to
                      detrimental, life-threatening metabolic disorders. SLC19A3
                      is furthermore a major site of drug interactions. Many
                      medications, including antidepressants, antibiotics and
                      chemotherapeutics are known to inhibit this transporter,
                      with potentially fatal consequences for patients. Despite a
                      thorough functional characterisation over the past two
                      decades, the structural basis of its transport mechanism and
                      drug interactions has remained elusive. Here, we report
                      seven cryo-electron microscopy (cryo-EM) structures of the
                      human thiamine transporter SLC19A3 in complex with various
                      ligands. Conformation-specific nanobodies enable us to
                      capture different states of SLC19A3’s transport cycle,
                      revealing the molecular details of thiamine recognition and
                      transport. We identify seven previously unknown drug
                      interactions of SLC19A3 and present structures of the
                      transporter in complex with the inhibitors fedratinib,
                      amprolium and hydroxychloroquine. These data allow us to
                      develop an understanding of the transport mechanism and
                      ligand recognition of SLC19A3.},
      cin          = {CSSB-EMBL-CL},
      ddc          = {500},
      cid          = {I:(DE-H253)CSSB-EMBL-CL-20210806},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39358356},
      UT           = {WOS:001327144400015},
      doi          = {10.1038/s41467-024-52872-8},
      url          = {https://bib-pubdb1.desy.de/record/615561},
}