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@ARTICLE{Marchiori:201309,
      author       = {Marchiori, Alessandro and Capece, Luciana and Giorgetti,
                      Alejandro and Gasparini, Paolo and Behrens, Maik and
                      Carloni, Paolo and Meyerhof, Wolfgang},
      title        = {{C}oarse-{G}rained/{M}olecular {M}echanics of the
                      {TAS}2{R}38 {B}itter {T}aste {R}eceptor:
                      {E}xperimentally-{V}alidated {D}etailed {S}tructural
                      {P}rediction of {A}gonist {B}inding},
      journal      = {PLoS one},
      volume       = {8},
      number       = {5},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2015-03614},
      pages        = {e64675 -},
      year         = {2013},
      abstract     = {Bitter molecules in humans are detected by ~25 G
                      protein-coupled receptors (GPCRs). The lack of atomic
                      resolution structure for any of them is complicating an in
                      depth understanding of the molecular mechanisms underlying
                      bitter taste perception. Here, we investigate the molecular
                      determinants of the interaction of the TAS2R38 bitter taste
                      receptor with its agonists phenylthiocarbamide (PTC) and
                      propylthiouracil (PROP). We use the recently developed
                      hybrid Molecular Mechanics/Coarse Grained (MM/CG) method
                      tailored specifically for GPCRs. The method, through an
                      extensive exploration of the conformational space in the
                      binding pocket, allows the identification of several
                      residues important for agonist binding that would have been
                      very difficult to capture from the standard
                      bioinformatics/docking approach. Our calculations suggest
                      that both agonists bind to Asn103, Phe197, Phe264 and
                      Trp201, whilst they do not interact with the so-called extra
                      cellular loop 2, involved in cis-retinal binding in the GPCR
                      rhodopsin. These predictions are consistent with data sets
                      based on more than 20 site-directed mutagenesis and
                      functional calcium imaging experiments of TAS2R38. The
                      method could be readily used for other GPCRs for which
                      experimental information is currently lacking},
      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:000319799900079},
      pubmed       = {pmid:23741366},
      doi          = {10.1371/journal.pone.0064675},
      url          = {https://juser.fz-juelich.de/record/201309},
}