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@ARTICLE{Cong:280667,
      author       = {Cong, Xiaojing and Campomanes, Pablo and Kless, Achim and
                      Schapitz, Inga and Wagener, Markus and Koch, Thomas and
                      Carloni, Paolo},
      title        = {{S}tructural {D}eterminants for the {B}inding of
                      {M}orphinan {A}gonists to the μ-{O}pioid {R}eceptor},
      journal      = {PLoS one},
      volume       = {10},
      number       = {8},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {FZJ-2016-00424},
      pages        = {e0135998 -},
      year         = {2015},
      abstract     = {Atomistic descriptions of the μ-opioid receptor (μOR)
                      noncovalently binding with two of its prototypical morphinan
                      agonists, morphine (MOP) and hydromorphone (HMP), are
                      investigated using molecular dynamics (MD) simulations.
                      Subtle differences between the binding modes and hydration
                      properties of MOP and HMP emerge from the calculations.
                      Alchemical free energy perturbation calculations show
                      qualitative agreement with in vitro experiments performed in
                      this work: indeed, the binding free energy difference
                      between MOP and HMP computed by forward and backward
                      alchemical transformation is 1.2±1.1 and 0.8±0.8 kcal/mol,
                      respectively, to be compared with 0.4±0.3 kcal/mol from
                      experiment. Comparison with an MD simulation of μOR
                      covalently bound with the antagonist β-funaltrexamine hints
                      to agonist-induced conformational changes associated with an
                      early event of the receptor’s activation: a shift of the
                      transmembrane helix 6 relative to the transmembrane helix 3
                      and a consequent loss of the key R165-T279 interhelical
                      hydrogen bond. This finding is consistent with a previous
                      proposal suggesting that the R165-T279 hydrogen bond between
                      these two helices indicates an inactive receptor
                      conformation.},
      cin          = {GRS Jülich ; German Research School for Simulation
                      Sciences / IAS-5 / INM-9},
      ddc          = {500},
      cid          = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330 /
                      I:(DE-Juel1)INM-9-20140121},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000359664300031},
      pubmed       = {pmid:26280453},
      doi          = {10.1371/journal.pone.0135998},
      url          = {https://juser.fz-juelich.de/record/280667},
}