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@ARTICLE{Suku:834631,
      author       = {Suku, Eda and Fierro, Fabrizio and Giorgetti, Alejandro and
                      Alfonso-Prieto, Mercedes and Carloni, Paolo},
      title        = {{M}ulti-scale simulations of membrane proteins: {T}he case
                      of bitter taste receptors},
      journal      = {Journal of science},
      volume       = {2},
      number       = {1},
      issn         = {2468-2179},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {FZJ-2017-04539},
      pages        = {15 - 21},
      year         = {2017},
      abstract     = {Human bitter taste receptors (hTAS2Rs) are the second
                      largest group of chemosensory G-protein coupled receptors
                      (25 members). hTAS2Rs are expressed in many tissues (e.g.
                      tongue, gastrointestinal tract, respiratory system, brain,
                      etc.), performing a variety of functions, from bitter taste
                      perception to hormone secretion and bronchodilation. Due to
                      the lack of experimental structural information,
                      computations are currently the methods of choice to get
                      insights into ligand–receptor interactions. Here we review
                      our efforts at predicting the binding pose of agonists to
                      hTAS2Rs, using state-of-the-art bioinformatics approaches
                      followed by hybrid Molecular Mechanics/Coarse-Grained
                      (MM/CG) simulations. The latter method, developed by us,
                      describes atomistically only the agonist binding region,
                      including hydration, and it may be particularly suited to be
                      used when bioinformatics predictions generate very
                      low-resolution models, such as the case of hTAS2Rs. Our
                      structural predictions of the hTAS2R38 and hTAS2R46
                      receptors in complex with their agonists turn out to be
                      fully consistent with experimental mutagenesis data. In
                      addition, they suggest a two-binding site architecture in
                      hTAS2R46, consisting of the usual orthosteric site together
                      with a “vestibular” site toward the extracellular space,
                      as observed in other GPCRs. The presence of the vestibular
                      site may help to discriminate among the wide spectrum of
                      bitter ligands},
      cin          = {IAS-5 / INM-9},
      ddc          = {600},
      cid          = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
      pnm          = {574 - Theory, modelling and simulation (POF3-574)},
      pid          = {G:(DE-HGF)POF3-574},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000407868100002},
      doi          = {10.1016/j.jsamd.2017.03.001},
      url          = {https://juser.fz-juelich.de/record/834631},
}