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@ARTICLE{Granzin:276150,
      author       = {Granzin, Joachim and Stadler, Andreas and Cousin, Anneliese
                      and Schlesinger, Ramona and Batra-Safferling, Renu},
      title        = {{S}tructural evidence for the role of polar core residue
                      {A}rg175 in arrestin activation},
      journal      = {Scientific reports},
      volume       = {5},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2015-06623},
      pages        = {15808},
      year         = {2015},
      abstract     = {Binding mechanism of arrestin requires photoactivation and
                      phosphorylation of the receptor protein rhodopsin, where the
                      receptor bound phosphate groups cause displacement of the
                      long C-tail ‘activating’ arrestin. Mutation of arginine
                      175 to glutamic acid (R175E), a central residue in the polar
                      core and previously predicted as the ‘phosphosensor’
                      leads to a pre-active arrestin that is able to terminate
                      phototransduction by binding to non-phosphorylated,
                      light-activated rhodopsin. Here, we report the first crystal
                      structure of a R175E mutant arrestin at 2.7 Å resolution
                      that reveals significant differences compared to the basal
                      state reported in full-length arrestin structures. These
                      differences comprise disruption of hydrogen bond network in
                      the polar core, and three-element interaction including
                      disordering of several residues in the receptor-binding
                      finger loop and the C-terminus (residues 361–404).
                      Additionally, R175E structure shows a 7.5° rotation of the
                      amino and carboxy-terminal domains relative to each other.
                      Consistent to the biochemical data, our structure suggests
                      an important role of R29 in the initial activation step of
                      C-tail release. Comparison of the crystal structures of
                      basal arrestin and R175E mutant provide insights into the
                      mechanism of arrestin activation, where binding of the
                      receptor likely induces structural changes mimicked as in
                      R175E.},
      cin          = {ICS-1 / Neutronenstreuung ; JCNS-1 / ICS-6},
      ddc          = {000},
      cid          = {I:(DE-Juel1)ICS-1-20110106 / I:(DE-Juel1)JCNS-1-20110106 /
                      I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
                      / 6215 - Soft Matter, Health and Life Sciences (POF3-621)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF3-6G4 /
                      G:(DE-HGF)POF3-6215},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000363624600001},
      doi          = {10.1038/srep15808},
      url          = {https://juser.fz-juelich.de/record/276150},
}