Publication Abstract from PubMed
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.
Tuning of a neuronal calcium sensor.,Weiergraber OH, Senin II, Zernii EY, Churumova VA, Kovaleva NA, Nazipova AA, Permyakov SE, Permyakov EA, Philippov PP, Granzin J, Koch KW J Biol Chem. 2006 Dec 8;281(49):37594-602. Epub 2006 Oct 2. PMID:17015448[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
