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@ARTICLE{Senin:30299,
      author       = {Senin, I. I. and Vaganova, S. A. and Weiergräber, O. H.
                      and Ergorov, N. S. and Philippov, P. P. and Koch, K.-W.},
      title        = {{F}unctional restoration of the {C}a2 -myristoyl switch in
                      a recoverin mutant},
      journal      = {Journal of molecular biology},
      volume       = {330},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PreJuSER-30299},
      pages        = {409 - 418},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Recoverin is a neuronal calcium sensor protein that plays a
                      crucial role in vertebrate phototransduction. It undergoes a
                      Ca2+-myristoyl switch when Ca2+ binds to its two functional
                      EF-hand motifs (EF-hands 2 and 3), each present in one of
                      recoverin's two domains. Impairment of Ca2+-binding in
                      recoverin leads to a disturbance of the Ca2+-myristoyl
                      switch and loss of its regulatory properties, i.e. inhibiton
                      of rhodopsin kinase. We have engineered recoverin mutants
                      with either of the two functional EF-hands disabled, but
                      with a functional Ca2+-binding site in EF-hand 4. While a
                      defect in EF-hand 2 could not be rescued by the additional
                      EF-hand 4, the impairment of EF-hand 3 was powerfully
                      compensated by Ca2+-binding to EF-hand 4. For example, the
                      myristoylated form of the latter mutant bound to membranes
                      in a Ca2+-dependent way and was able to inhibit rhodopsin
                      kinase in a way similar to that of the wild-type protein.
                      Thus, for recoverin to undergo a Ca2+-myristoyl switch, it
                      is necessary and sufficient to have either of the two
                      EF-hands in the second domain in a functional state. On the
                      basis of these results and inspection of published
                      three-dimensional structures of recoverin, we propose a
                      model highlighting the mutual interdependence of sterical
                      configurations in EF-hands 3 and 4 of recoverin. (C) 2003
                      Elsevier Science Ltd. All rights reserved.},
      keywords     = {J (WoSType)},
      cin          = {IBI-1 / IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB57 / I:(DE-Juel1)VDB58},
      pnm          = {Neurowissenschaften},
      pid          = {G:(DE-Juel1)FUEK255},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000183824900020},
      doi          = {10.1016/S0022-2836(03)00581-3},
      url          = {https://juser.fz-juelich.de/record/30299},
}