Document Type
Article
Date
1998
Keywords
Amino Acid Substitution, Animals, Arginine, Cloning Molecular, Escherichia coli, Eye Proteins/chemistry, Eye Proteins/metabolism, Eye Proteins/physiology, Gene Expression, Glutamine, Mutagenesis Site-Directed, Recombinant Fusion Proteins, Retinol-Binding Proteins/chemistry, Retinol-Binding Proteins/metabolism, Retinol-Binding Proteins/physiology, Stearic Acids/pharmacokinetics, Vitamin A/pharmacokinetics, Xenopus
Language
English
Disciplines
Chemistry
Description/Abstract
Interphotoreceptor retinoid-binding protein (IRBP) is unusual for a lipid-binding protein in that its gene is expressed uniquely by cells of photoreceptor origin and consists of four homologous repeats, each coding for a module of~300 amino acid residues. All-trans retinol binding domains, which appear to be present in each module, are composed of conserved hydrophobic regions [Baer et al, Exp Eye Res 1998; 66:249-262]. Here we investigate the role of highly conserved arginines contained in these regions.
Recommended Citation
Baer, C A & Van Niel, E E & Cronk, J W & Kinter, M T & Sherman, N E & Braiman, M S & Gonzalez-Fernandez, F. (1998). Arginine to glutamine substitutions in the fourth module of Xenopus interphotoreceptor retinoid-binding protein. Molecular vision, 4. Retreived from http://www.biomedsearch.com/nih/Arginine-to-glutamine-substitutions-in/9873068.html
