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@ARTICLE{Feuerstein:7146,
      author       = {Feuerstein, S.E. and Pulvermüller, A. and Hartmann, R. and
                      Granzin, J. and Stoldt, M. and Henklein, P. and Ernst, O.P.
                      and Heck, M. and Willbold, D. and Koenig, B. W.},
      title        = {{H}elix {F}ormation in {A}rrestin {A}ccompanies
                      {R}ecognition of {P}hotoactivated {R}hodopsin},
      journal      = {Biochemistry},
      volume       = {48},
      issn         = {0006-2960},
      address      = {Columbus, Ohio},
      publisher    = {American Chemical Society},
      reportid     = {PreJuSER-7146},
      pages        = {10733 -10742},
      year         = {2009},
      note         = {This work was supported by grants from the Deutsche
                      Forschungsgemeinschaft (DFG) to B.W.K. (Ko 2143/3), AR (Pu
                      186/3), and O.P. E. (Er 294/1).},
      abstract     = {Binding of arrestin to photoactivated phosphorylated
                      rhodopsin terminates the amplification of visual signals in
                      photoreceptor cells. Currently, there is no crystal
                      structure of a rhodopsin-arrestin complex available,
                      although structures of unbound rhodopsin and arrestin have
                      been determined. High-affinity receptor binding is dependent
                      on distinct arrestin sites responsible for recognition of
                      rhodopsin activation and phosphorylation. The loop
                      connecting beta-strands V and VI in rod arrestin has been
                      implicated in the recognition of active rhodopsin. We report
                      the structure of receptor-bound arrestin peptide Arr(67-77)
                      mimicking this loop based on solution NMR data. The peptide
                      binds photoactivated rhodopsin in the unphosphorylated and
                      phosphorylated form with similar affinities and stabilizes
                      the metarhodopsin II photointermediate. A largely
                      alpha-helical conformation of the receptor-bound peptide is
                      observed.},
      keywords     = {Arrestin: chemistry / Models, Molecular / Nuclear Magnetic
                      Resonance, Biomolecular / Photochemistry / Protein
                      Conformation / Rhodopsin: chemistry / Arrestin (NLM
                      Chemicals) / Rhodopsin (NLM Chemicals) / J (WoSType)},
      cin          = {ISB-3},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB942},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19835414},
      UT           = {WOS:000271459100009},
      doi          = {10.1021/bi900544p},
      url          = {https://juser.fz-juelich.de/record/7146},
}