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@ARTICLE{Skegro:57375,
      author       = {Skegro, D. and Pulvermuller, A. and Krafft, B. and Granzin,
                      J. and Hofmann, K. P. and Büldt, G. and Schlesinger, R.},
      title        = {{N}-terminal and {C}-terminal {D}omains of {A}rrestin
                      {B}oth {C}ontribute in {B}inding to {R}hodopsin (dagger)},
      journal      = {Photochemistry and photobiology},
      volume       = {83},
      issn         = {0031-8655},
      address      = {Malden, Mass.},
      publisher    = {Wiley-Blackwell},
      reportid     = {PreJuSER-57375},
      pages        = {385 - 393},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Visual arrestin terminates the signal amplification cascade
                      in photoreceptor cells by blocking the interaction of light
                      activated phosphorylated rhodopsin with the G-protein
                      transducin. Although crystal structures of arrestin and
                      rhodopsin are available, it is still unknown how the complex
                      of the two proteins is formed. To investigate the
                      interaction sites of arrestin with rhodopsin various surface
                      regions of recombinant arrestin were sterically blocked by
                      different numbers of fluorophores (Alexa 633). The binding
                      was recorded by time-resolved light scattering. To
                      accomplish site-specific shielding of protein regions, in a
                      first step all three wild-type cysteines were replaced by
                      alanines. Nevertheless, regarding the magnitude and
                      specificity of rhodopsin binding, the protein is still fully
                      active. In a second step, new cysteines were introduced at
                      selected sites to allow covalent binding of fluorophores.
                      Upon attachment of Alexa 633 to the recombinant cysteines we
                      observed that these bulky labels residing in the concave
                      area of either the N- or the C-terminal domain do not
                      perturb the activity of arrestin. By simultaneously
                      modifying both domains with one Alexa 633 the binding
                      capacity was reduced. The presence of two Alexa 633
                      molecules in each domain prevented binding of rhodopsin to
                      arrestin. This observation indicates that both concave sites
                      participate in binding.},
      keywords     = {Animals / Arrestin: chemistry / Arrestin: genetics /
                      Arrestin: metabolism / Base Sequence / Binding Sites /
                      Cattle / Cysteine: chemistry / DNA Primers: genetics /
                      Fluorescent Dyes / Models, Molecular / Mutagenesis,
                      Site-Directed / Photochemistry / Protein Binding / Protein
                      Structure, Tertiary / Recombinant Proteins: chemistry /
                      Recombinant Proteins: genetics / Recombinant Proteins:
                      metabolism / Rhodopsin: metabolism / Signal Transduction /
                      Arrestin (NLM Chemicals) / DNA Primers (NLM Chemicals) /
                      Fluorescent Dyes (NLM Chemicals) / Recombinant Proteins (NLM
                      Chemicals) / Cysteine (NLM Chemicals) / Rhodopsin (NLM
                      Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Biophysics},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17132044},
      UT           = {WOS:000245658000025},
      doi          = {10.1562/2006-08-25-RA-1014},
      url          = {https://juser.fz-juelich.de/record/57375},
}