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@ARTICLE{Kondo:632990,
      author       = {Kondo, Yasushi and Hatton, Caitlin and Cheng, Robert and
                      Trabuco, Matilde and Glover, Hannah and Bertrand, Quentin
                      and Stierli, Fabienne and Seidel, Hans-Peter and Mason,
                      Thomas and Sarma, Sivathmika and Tellkamp, Friedjof and
                      Kepa, Michal and Dworkowski, Florian and Mehrabi, Pedram and
                      Hennig, Michael and Standfuss, Joerg},
      title        = {{A}po‐state structure of the metabotropic glutamate
                      receptor 5 transmembrane domain obtained using a
                      photoswitchable ligand},
      journal      = {Protein science},
      volume       = {34},
      number       = {7},
      issn         = {0961-8368},
      address      = {Hoboken, NJ},
      publisher    = {Wiley},
      reportid     = {PUBDB-2025-02316},
      pages        = {e70104},
      year         = {2025},
      abstract     = {Metabotropic glutamate receptor 5 (mGlu5) is implicated in
                      various neurodegenerative disorders, making it an attractive
                      drug target. Although several ligand-bound crystal
                      structures of mGlu5 exist, their apo-state crystal structure
                      remains unknown. Here, we study mGlu5 structural changes
                      using the photochemical affinity switch, alloswitch-1, in
                      combination with time-resolved freeze-trapping methods. By
                      X-ray crystallography, we demonstrated that isomerizing
                      alloswitch-1 leads to its release from the binding pocket
                      within a few seconds. The apo structure, determined at a
                      resolution of 2.9 Å, is more comparable to the inactive
                      state than to the active state. Our approach presents an
                      accessible alternative to time-resolved serial
                      crystallography for capturing thermodynamically stable
                      transient intermediates. The mGlu5 apo-structure provides
                      molecular insights into the ligand-free allosteric pocket,
                      which can guide the design of new allosteric modulators.},
      cin          = {EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project
                      G:(GEPRIS)451079909 - Untersuchung allosterischer
                      Mechanismen durch zeitaufgelöste serielle
                      Synchrotronkristallographie (451079909)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)451079909},
      experiment   = {EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40521617},
      doi          = {10.1002/pro.70104},
      url          = {https://bib-pubdb1.desy.de/record/632990},
}