% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Biarns:201341,
      author       = {Biarnés, Xevi and Marchiori, Alessandro and Giorgetti,
                      Alejandro and Lanzara, Carmela and Gasparini, Paolo and
                      Carloni, Paolo and Born, Stephan and Brockhoff, Anne and
                      Behrens, Maik and Meyerhof, Wolfgang},
      title        = {{I}nsights into the {B}inding of {P}henyltiocarbamide
                      ({PTC}) {A}gonist to {I}ts {T}arget {H}uman {TAS}2{R}38
                      {B}itter {R}eceptor},
      journal      = {PLoS one},
      volume       = {5},
      number       = {8},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2015-03638},
      pages        = {e12394 -},
      year         = {2010},
      abstract     = {Humans' bitter taste perception is mediated by the hTAS2R
                      subfamily of the G protein-coupled membrane receptors
                      (GPCRs). Structural information on these receptors is
                      currently limited. Here we identify residues involved in the
                      binding of phenylthiocarbamide (PTC) and in receptor
                      activation in one of the most widely studied hTAS2Rs
                      (hTAS2R38) by means of structural bioinformatics and
                      molecular docking. The predictions are validated by
                      site-directed mutagenesis experiments that involve specific
                      residues located in the putative binding site and
                      trans-membrane (TM) helices 6 and 7 putatively involved in
                      receptor activation. Based on our measurements, we suggest
                      that (i) residue N103 participates actively in PTC binding,
                      in line with previous computational studies. (ii) W99, M100
                      and S259 contribute to define the size and shape of the
                      binding cavity. (iii) W99 and M100, along with F255 and
                      V296, play a key role for receptor activation, providing
                      insights on bitter taste receptor activation not emerging
                      from the previously reported computational models.},
      cin          = {GRS / IAS-5},
      ddc          = {500},
      cid          = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
      pnm          = {899 - ohne Topic (POF2-899)},
      pid          = {G:(DE-HGF)POF2-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000281234700019},
      pubmed       = {20811630},
      doi          = {10.1371/journal.pone.0012394},
      url          = {https://juser.fz-juelich.de/record/201341},
}