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@ARTICLE{Weiergrber:54334,
      author       = {Weiergräber, O. H. and Senin, I. I. and Zernii, E.Y. and
                      Churumova, V. A. and Kovaleva, N. A. and Nazipova, A. A. and
                      Permyakov, S.E. and Permyakov, E.A. and Philippov, P.P. and
                      Granzin, J. and Koch, K. W.},
      title        = {{T}uning of a neuronal calcium sensor},
      journal      = {The journal of biological chemistry},
      volume       = {281},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-54334},
      pages        = {37594 - 37602},
      year         = {2006},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Recoverin is a Ca(2+)-regulated signal transduction
                      modulator expressed in the vertebrate retina that has been
                      implicated in visual adaptation. An intriguing feature of
                      recoverin is a cluster of charged residues at its C
                      terminus, the functional significance of which is largely
                      unclear. To elucidate the impact of this segment on
                      recoverin structure and function, we have investigated a
                      mutant lacking the C-terminal 12 amino acids. Whereas in
                      myristoylated recoverin the truncation causes an overall
                      decrease in Ca(2+) sensitivity, results for the
                      non-myristoylated mutant indicate that the truncation
                      primarily affects the high affinity EF-hand 3. The
                      three-dimensional structure of the mutant has been
                      determined by x-ray crystallography. In addition to
                      significant changes in average coordinates compared with
                      wild-type recoverin, the structure provides strong
                      indication of increased conformational flexibility,
                      particularly in the C-terminal domain. Based on these
                      observations, we propose a novel role of the C-terminal
                      segment of recoverin as an internal modulator of Ca(2+)
                      sensitivity.},
      keywords     = {Animals / Base Sequence / Calcium Signaling: physiology /
                      Cattle / Crystallography, X-Ray / DNA Primers: genetics /
                      Kinetics / Models, Molecular / Mutagenesis, Site-Directed /
                      Protein Structure, Quaternary / Recombinant Proteins:
                      chemistry / Recombinant Proteins: genetics / Recombinant
                      Proteins: metabolism / Recoverin: chemistry / Recoverin:
                      genetics / Recoverin: metabolism / Rod Cell Outer Segment:
                      metabolism / Sequence Deletion / Surface Plasmon Resonance /
                      DNA Primers (NLM Chemicals) / RCV1 protein, Bos taurus (NLM
                      Chemicals) / Recombinant Proteins (NLM Chemicals) /
                      Recoverin (NLM Chemicals) / J (WoSType)},
      cin          = {IBI-2},
      ddc          = {570},
      cid          = {I:(DE-Juel1)VDB58},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Biochemistry $\&$ Molecular Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17015448},
      UT           = {WOS:000242477100036},
      doi          = {10.1074/jbc.M603700200},
      url          = {https://juser.fz-juelich.de/record/54334},
}