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@ARTICLE{Amundarain:861857,
      author       = {Amundarain, María Julia and Viso, Juan Francisco and
                      Zamarreño, Fernando and Giorgetti, Alejandro and Costabel,
                      Marcelo},
      title        = {{O}rthosteric and benzodiazepine cavities of the α 1 β 2
                      γ 2 {GABA} {A} receptor: insights from experimentally
                      validated in silico methods},
      journal      = {Journal of biomolecular structure $\&$ dynamics},
      volume       = {37},
      number       = {6},
      issn         = {0739-1102},
      address      = {Abingdon [u.a.]},
      publisher    = {Taylor $\&$ Francis},
      reportid     = {FZJ-2019-02278},
      pages        = {1597 - 1615},
      year         = {2019},
      abstract     = {γ-aminobutyric acid-type A (GABAA) receptors mediate fast
                      synaptic inhibition in the central nervous system of
                      mammals. They are modulated via several sites by numerous
                      compounds, which include GABA, benzodiazepines, ethanol,
                      neurosteroids and anaesthetics among others. Due to their
                      potential as targets of novel drugs, a detailed knowledge of
                      their structure-function relationships is needed. Here, we
                      present the model of the α1β2γ2 subtype GABAA receptor in
                      the APO state and in complex with selected ligands,
                      including agonists, antagonists and allosteric modulators.
                      The model is based on the crystallographic structure of the
                      human β3 homopentamer GABAA receptor. The complexes were
                      refined using atomistic molecular dynamics simulations. This
                      allowed a broad description of the binding modes and the
                      detection of important interactions in agreement with
                      experimental information. From the best of our knowledge,
                      this is the only model of the α1β2γ2 GABAA receptor that
                      represents altogether the desensitized state of the channel
                      and comprehensively describes the interactions of ligands of
                      the orthosteric and benzodiazepines binding sites in
                      agreement with the available experimental data. Furthermore,
                      it is able to explain small differences regarding the
                      binding of a variety of chemically divergent ligands.
                      Finally, this new model may pave the way for the design of
                      focused experimental studies that will allow a deeper
                      description of the receptor.},
      cin          = {IAS-5 / INM-9},
      ddc          = {570},
      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},
      pubmed       = {pmid:29633901},
      UT           = {WOS:000461434300018},
      doi          = {10.1080/07391102.2018.1462733},
      url          = {https://juser.fz-juelich.de/record/861857},
}