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@ARTICLE{Wifling:865162,
      author       = {Wifling, David and Pfleger, Christopher and Kaindl, Jonas
                      and Ibrahim, Paissante and Kling, Ralf and Buschauer, Armin
                      and Gohlke, Holger and Clark, Tim},
      title        = {{B}asal {H}istamine {H}4 {R}eceptor {A}ctivation: {A}gonist
                      {M}imicry by the {D}iphenylalanine {M}otif},
      journal      = {Chemistry - a European journal},
      volume       = {25},
      number       = {64},
      issn         = {1521-3765},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2019-04708},
      pages        = {14613-14624},
      year         = {2019},
      abstract     = {Histamine H4 receptor (H4R) orthologues are G‐protein
                      coupled receptors (GPCRs) that exhibit species‐dependent
                      basal activity: In contrast to the basally inactive mouse
                      H4R (mH4R), human H4R (hH4R) shows a high degree of basal
                      activity. We have performed long‐time‐scale
                      molecular‐dynamics simulations and rigidity analyses on
                      wild‐type hH4R, the experimentally characterized hH4R
                      variants S179M, F169V, F169V+S179M, F168A, and on mH4R to
                      investigate the molecular nature of differential basal
                      activity. H4R variant‐dependent differences between
                      essential motifs of GPCR activation and structural
                      stabilities correlate with experimentally determined basal
                      activities and provide a molecular explanation for the
                      differences in basal activation. Strikingly, during the MD
                      simulations, F16945.55 dips into the orthosteric binding
                      pocket only in the case of hH4R, thus adopting the role of
                      an agonist and contributing to the stabilization of the
                      active state. The results shed new light on the molecular
                      mechanism of basal H4R activation that are of importance for
                      other GPCRs.},
      cin          = {NIC / JSC / ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)NIC-20090406 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)ICS-6-20110106},
      pnm          = {511 - Computational Science and Mathematical Methods
                      (POF3-511) / Forschergruppe Gohlke $(hkf7_20170501)$},
      pid          = {G:(DE-HGF)POF3-511 / $G:(DE-Juel1)hkf7_20170501$},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:31498478},
      UT           = {WOS:000490306500001},
      doi          = {10.1002/chem.201902801},
      url          = {https://juser.fz-juelich.de/record/865162},
}