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@ARTICLE{Sandal:205116,
      author       = {Sandal, Massimo and Behrens, Maik and Brockhoff, Anne and
                      Musiani, Francesco and Giorgetti, Alejandro and Carloni,
                      Paolo and Meyerhof, Wolfgang},
      title        = {{E}vidence for a {T}ransient {A}dditional {L}igand
                      {B}inding {S}ite in the {TAS}2{R}46 {B}itter {T}aste
                      {R}eceptor},
      journal      = {Journal of chemical theory and computation},
      volume       = {11},
      number       = {9},
      issn         = {1549-9626},
      address      = {Washington, DC},
      publisher    = {American Chemical Society (ACS)},
      reportid     = {FZJ-2015-05586},
      pages        = {4439 - 4449},
      year         = {2015},
      abstract     = {Most human G protein coupled receptors (GPCRs) are
                      activated by small molecules binding to their
                      7-transmembrane (7-TM) helix bundle. They belong to basally
                      diverging branches: the 25 bitter taste 2 receptors and most
                      members of the very large rhodopsin-like/class A GPCRs
                      subfamily. Some members of the class A branch have been
                      suggested to feature not only an orthosteric agonist-binding
                      site but also a more extracellular or “vestibular” site,
                      involved in the binding process. Here we use a hybrid
                      molecular mechanics/coarse-grained (MM/CG) molecular
                      dynamics approach on a widely studied bitter taste receptor
                      (TAS2R46) receptor in complex with its agonist strychnine.
                      Three ∼1 μs molecular simulation trajectories find two
                      sites hosting the agonist, which together elucidate
                      experimental data measured previously and in this work. This
                      mechanism shares similarities with the one suggested for the
                      evolutionarily distant class A GPCRs. It might be
                      instrumental for the remarkably broad but specific spectrum
                      of agonists of these chemosensory receptors.},
      cin          = {GRS / IAS-5 / INM-9},
      ddc          = {540},
      cid          = {I:(DE-Juel1)GRS-20100316 / 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:000361087600046},
      pubmed       = {pmid:26575934},
      doi          = {10.1021/acs.jctc.5b00472},
      url          = {https://juser.fz-juelich.de/record/205116},
}