Home > Publications database > Tuning of a neuronal calcium sensor |
Journal Article | PreJuSER-54334 |
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2006
Soc.
Bethesda, Md.
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Please use a persistent id in citations: http://hdl.handle.net/2128/2657 doi:10.1074/jbc.M603700200
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.
Keyword(s): Animals (MeSH) ; Base Sequence (MeSH) ; Calcium Signaling: physiology (MeSH) ; Cattle (MeSH) ; Crystallography, X-Ray (MeSH) ; DNA Primers: genetics (MeSH) ; Kinetics (MeSH) ; Models, Molecular (MeSH) ; Mutagenesis, Site-Directed (MeSH) ; Protein Structure, Quaternary (MeSH) ; Recombinant Proteins: chemistry (MeSH) ; Recombinant Proteins: genetics (MeSH) ; Recombinant Proteins: metabolism (MeSH) ; Recoverin: chemistry (MeSH) ; Recoverin: genetics (MeSH) ; Recoverin: metabolism (MeSH) ; Rod Cell Outer Segment: metabolism (MeSH) ; Sequence Deletion (MeSH) ; Surface Plasmon Resonance (MeSH) ; DNA Primers ; RCV1 protein, Bos taurus ; Recombinant Proteins ; Recoverin ; J
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