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@ARTICLE{Weiergrber:30298,
      author       = {Weiergräber, O. H. and Senin, I. I. and Philippov, P. P.
                      and Granzin, J. and Koch, K.-W.},
      title        = {{I}mpact of {N}-terminal myristoylation on the
                      {C}a2+-dependent conformational transition in recoverin},
      journal      = {The journal of biological chemistry},
      volume       = {278},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PreJuSER-30298},
      pages        = {22972 - 22979},
      year         = {2003},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Recoverin is a Ca2+-regulated signal transduction modulator
                      found in vertebrate retina that has been shown to undergo
                      dramatic conformational changes upon Ca2+ binding to its two
                      functional EF-hand motifs. To elucidate the differential
                      impact of the N-terminal myristoylation as well as
                      occupation of the two Ca2+ binding sites on recoverin
                      structure and function, we have investigated a
                      non-myristoylated E85Q mutant exhibiting virtually no Ca2+
                      binding to EF-2. Crystal structures of the mutant protein as
                      well as the non-myristoylated wild-type have been
                      determined. Although the non-myristoylated E85Q mutant does
                      not display any functional activity, its three-dimensional
                      structure in the presence of Ca2+ resembles the
                      myristoylated wild-type with two Ca2+ but is quite
                      dissimilar from the myristoylated E85Q mutant. We conclude
                      that the N-terminal myristoyl modification significantly
                      stabilizes the conformation of the Ca2+-free protein (i.e.
                      the T conformation) during the stepwise transition toward
                      the fully Ca2+-occupied state. On the basis of these
                      observations, a refined model for the role of the myristoyl
                      group as an intrinsic allosteric modulator is proposed.},
      keywords     = {Amino Acid Substitution / Animals / Calcium: metabolism /
                      Calcium-Binding Proteins: chemistry / Calcium-Binding
                      Proteins: metabolism / Cattle / Crystallography, X-Ray / Eye
                      Proteins / G-Protein-Coupled Receptor Kinase 1 / Hippocalcin
                      / Kinetics / Lipoproteins / Models, Molecular / Mutagenesis,
                      Site-Directed / Myristic Acid: metabolism / Nerve Tissue
                      Proteins / Protein Binding / Protein Conformation / Protein
                      Kinases: metabolism / Protein Structure, Secondary /
                      Recombinant Proteins: chemistry / Recombinant Proteins:
                      metabolism / Recoverin / Rod Cell Outer Segment: metabolism
                      / Tumor Markers, Biological: chemistry / Tumor Markers,
                      Biological: metabolism / Calcium-Binding Proteins (NLM
                      Chemicals) / Eye Proteins (NLM Chemicals) / Lipoproteins
                      (NLM Chemicals) / Nerve Tissue Proteins (NLM Chemicals) /
                      Recombinant Proteins (NLM Chemicals) / Tumor Markers,
                      Biological (NLM Chemicals) / Recoverin (NLM Chemicals) /
                      Hippocalcin (NLM Chemicals) / Myristic Acid (NLM Chemicals)
                      / Calcium (NLM Chemicals) / Protein Kinases (NLM Chemicals)
                      / G-Protein-Coupled Receptor Kinase 1 (NLM Chemicals) / 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},
      pubmed       = {pmid:12686556},
      UT           = {WOS:000183503900104},
      doi          = {10.1074/jbc.M300447200},
      url          = {https://juser.fz-juelich.de/record/30298},
}