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FEBS Lett ; 440(1-2): 116-8, 1998 Nov 27.
Article in English | MEDLINE | ID: mdl-9862438

ABSTRACT

Several EF-hand recoverin mutants were obtained and their abilities to bind to photoreceptor membranes and to inhibit rhodopsin kinase were determined. The mutants with the 'spoiled' 2nd, 3rd or (2nd+3rd) EF-hand structures did not act upon the kinase activity in the microM range of Ca2+ concentrations. Mutations of the 4th EF hand, which 'repaired' its Ca2+-binding activity, resulted in recoverin with three 'working' Ca2+-binding sites. The latter mutant inhibited rhodopsin kinase even more effectively than the wild-type recoverin, containing two working Ca2+-binding structures.


Subject(s)
Calcium-Binding Proteins/genetics , Calcium-Binding Proteins/metabolism , Eye Proteins , Lipoproteins , Mutation , Nerve Tissue Proteins , Protein Kinase Inhibitors , Protein Kinases , Rod Cell Outer Segment/metabolism , Animals , Binding Sites , Calcium/metabolism , Calcium-Binding Proteins/chemistry , Cattle , G-Protein-Coupled Receptor Kinase 1 , Hippocalcin , Mutagenesis, Site-Directed , Phenotype , Phosphorylation , Protein Structure, Secondary , Recoverin , Retina
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