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@ARTICLE{Granzin:111980,
      author       = {Granzin, J. and Cousin, A. and Weirauch, M. and
                      Schlesinger, R. and Büldt, G. and Batra-Safferling, R.},
      title        = {{C}rystal structure of p44, a constitutively active splice
                      variant of visual arrestin},
      journal      = {Journal of molecular biology},
      volume       = {416},
      number       = {5},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-111980},
      pages        = {611 - 618},
      year         = {2012},
      note         = {We are grateful to the beamline scientists at the European
                      Synchrotron Radiation Facility (Grenoble, France) for
                      providing assistance with the use of beamline ID14-4. We
                      thank Oliver H. Weiergraber for comments on the manuscript,
                      Bianca Krafft for generating the p44 clone in S. cerevisiae,
                      and Dieter Willbold and the Russian Group ONEXIM (GB) for
                      generous support.},
      abstract     = {Visual arrestin specifically binds to photoactivated and
                      phosphorylated rhodopsin and inactivates phototransduction.
                      In contrast, the p44 splice variant can terminate
                      phototransduction by binding to nonphosphorylated
                      light-activated rhodopsin. Here we report the crystal
                      structure of bovine p44 at a resolution of 1.85 Å. Compared
                      to native arrestin, the p44 structure reveals significant
                      differences in regions crucial for receptor binding, namely
                      flexible loop V-VI and polar core regions. Additionally,
                      electrostatic potential is remarkably positive on the
                      N-domain and the C-domain. The p44 structure represents an
                      active conformation that serves as a model to explain the
                      'constitutive activity' found in arrestin variants.},
      keywords     = {Animals / Arrestin: chemistry / Arrestin: genetics /
                      Arrestin: metabolism / Cattle / Crystallography, X-Ray:
                      methods / Genetic Variation / Light Signal Transduction /
                      Models, Molecular / Phosphorylation / Protein Binding /
                      Protein Structure, Tertiary: genetics / RNA Splicing /
                      Rhodopsin: metabolism / Static Electricity / Arrestin (NLM
                      Chemicals) / Rhodopsin (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-5 / ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-5-20110106 / I:(DE-Juel1)ICS-6-20110106},
      pnm          = {BioSoft: Makromolekulare Systeme und biologische
                      Informationsverarbeitung / Funktion und Dysfunktion des
                      Nervensystems},
      pid          = {G:(DE-Juel1)FUEK505 / G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22306737},
      UT           = {WOS:000301682800001},
      doi          = {10.1016/j.jmb.2012.01.028},
      url          = {https://juser.fz-juelich.de/record/111980},
}