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@ARTICLE{Sharma:849921,
      author       = {Sharma, Kanika and Balfanz, Sabine and Baumann, Arnd and
                      Korsching, Sigrun},
      title        = {{F}ull rescue of an inactive olfactory receptor mutant by
                      elimination of an allosteric ligand-gating site},
      journal      = {Scientific reports},
      volume       = {8},
      number       = {1},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2018-04017},
      pages        = {9631},
      year         = {2018},
      abstract     = {Ligand-gating has recently been proposed as a novel
                      mechanism to regulate olfactory receptor sensitivity.
                      TAAR13c, the zebrafish olfactory receptor activated by the
                      death-associated odor cadaverine, appears to possess an
                      allosteric binding site for cadaverine, which was assumed to
                      block progress of the ligand towards the internal
                      orthosteric binding-and-activation site. Here we have
                      challenged the suggested gating mechanism by modeling the
                      entry tunnel for the ligand as well as the ligand path
                      inside the receptor. We report an entry tunnel, whose
                      opening is blocked by occupation of the external binding
                      site by cadaverine, confirming the hypothesized gating
                      mechanism. A multistep docking algorithm suggested a
                      plausible path for cadaverine from the allosteric to the
                      orthosteric binding-and-activation site. Furthermore we have
                      combined a gain-of-function gating site mutation and a
                      loss-of-function internal binding site mutation in one
                      recombinant receptor. This receptor had almost wildtype
                      ligand affinities, consistent with modeling results that
                      showed localized effects for each mutation. A novel mutation
                      of the suggested gating site resulted in increased receptor
                      ligand affinity. In summary both the experimental and the
                      modeling results provide further evidence for the proposed
                      gating mechanism, which surprisingly exhibits pronounced
                      similarity to processes described for some metabotropic
                      neurotransmitter receptors.},
      cin          = {ICS-4},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ICS-4-20110106},
      pnm          = {552 - Engineering Cell Function (POF3-552)},
      pid          = {G:(DE-HGF)POF3-552},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29941999},
      UT           = {WOS:000436077800052},
      doi          = {10.1038/s41598-018-27790-7},
      url          = {https://juser.fz-juelich.de/record/849921},
}