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@ARTICLE{Komolov:136533,
      author       = {Komolov, K. E. and Zinchenko, D. V. and Churumova, V. A.
                      and Vaganova, S. A. and Weiergräber, Oliver H. and Senin,
                      I. I. and Philippov, P. P. and Koch, K. W.},
      title        = {{O}ne of the {C}a(2+) binding sites of recoverin
                      exclusively controls interaction with rhodopsin kinase},
      journal      = {Biological chemistry},
      volume       = {386},
      issn         = {1431-6730},
      address      = {Berlin [u.a.]},
      publisher    = {de Gruyter},
      reportid     = {FZJ-2013-03329},
      pages        = {285-286},
      year         = {2005},
      abstract     = {Recoverin is a neuronal calcium sensor protein that
                      controls the activity of rhodopsin kinase in a
                      Ca(2+)-dependent manner. Mutations in the EF-hand Ca2+
                      binding sites are valuable tools for investigating the
                      functional properties of recoverin. In the recoverin mutant
                      E121Q (Rec E121Q ) the high-affinity Ca2+ binding site is
                      disabled. The non-myristoylated form of Rec E121Q binds one
                      Ca2+ via its second Ca(2+)-binding site (EF-hand 2), whereas
                      the myristoylated variant does not bind Ca2+ at all. Binding
                      of Ca2+ to non-myristoylated Rec E121Q apparently triggers
                      exposure of apolar side chains, allowing for association
                      with hydrophobic matrices. Likewise, an interaction surface
                      for the recoverin target rhodopsin kinase is constituted
                      upon Ca2+ binding to the non-acylated mutant. Structural
                      changes resulting from Ca(2+)-occupation of EF-hand 2 in
                      myristoylated and non-myristoylated recoverin variants are
                      discussed in terms of critical conditions required for
                      biological activity.},
      cin          = {ICS-6},
      ddc          = {540},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000228131400011},
      doi          = {10.1515/BC.2005.034},
      url          = {https://juser.fz-juelich.de/record/136533},
}