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@INBOOK{BatraSafferling:834100,
      author       = {Batra-Safferling, Renu and Granzin, Joachim},
      title        = {{T}he {S}tructure of the {P}olar {C}ore {M}utant {R}175{E}
                      and {I}ts {F}unctional {I}mplications},
      address      = {Cham},
      publisher    = {Springer International Publishing},
      reportid     = {FZJ-2017-04101},
      isbn         = {978-3-319-57553-7},
      pages        = {143-158},
      year         = {2017},
      comment      = {The Structural Basis of Arrestin Functions},
      booktitle     = {The Structural Basis of Arrestin
                       Functions},
      abstract     = {Mutation of arginine 175 to glutamic acid (R175E), a
                      central residue in the polar core and previously predicted
                      as the ‘phosphosensor’, leads to a constitutively active
                      arrestin that is able to terminate phototransduction by
                      binding to non-phosphorylated, light-activated rhodopsin .
                      Crystal structure of a R175E mutant arrestin at 2.7 Å
                      resolution reveals significant differences compared to the
                      basal state reported in full-length arrestin structures.
                      Most striking differences are disruption of hydrogen bond
                      network in the polar core , and three-element interaction
                      (between β-strand I, α-helix I, and the C-tail), 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.
                      Comparison of the crystal structures of basal arrestin and
                      R175E mutant provides insights into the mechanism of
                      arrestin activation, where the latter likely represents an
                      intermediate activation state prior to formation of the
                      high-affinity complex with the G protein-coupled receptor.},
      cin          = {ICS-6},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551)},
      pid          = {G:(DE-HGF)POF3-551},
      typ          = {PUB:(DE-HGF)7},
      doi          = {10.1007/978-3-319-57553-7_11},
      url          = {https://juser.fz-juelich.de/record/834100},
}