Differential binding of retinol analogs to two homologous cellular retinol-binding proteins

Autor:	Ding Rong, Andre d'Avignon, M. Rosenberger, A. J. Lovey, E. Li, Jay W. Ponder
Rok vydání:	1993
Předmět:	Stereochemistry Binding protein Retinol Cell Biology Ring (chemistry) Polyene Ligand (biochemistry) Biochemistry Fluorescence Retinol binding protein chemistry.chemical_compound chemistry Moiety Molecular Biology
Zdroj:	Journal of Biological Chemistry. 268:7929-7934
ISSN:	0021-9258
DOI:	10.1016/s0021-9258(18)53047-7
Popis:	A comparative study of the interactions of rat cellular retinol-binding protein (CRBP) and cellular retinol-binding protein II (CRBP II) with a number of synthetic phenyl-substituted analogs of all-trans-retinol was performed using fluorescence and nuclear magnetic resonance analysis. These studies indicate that CRBP II is more sensitive to modifications of the ring moiety than CRBP. Removal of the two methyl substituents on the ring which are ortho to the polyene chain abolishes binding to CRBP II. Conformational analysis of the ligands indicates that these two methyl groups influence the planarity of the ligand. The identification of monospecific ligands may prove useful for studying the physiological roles of these two proteins.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::c9ca877b2f6ed30917429c608f9b4cd9 https://doi.org/10.1016/s0021-9258(18)53047-7 Zobrazit plný text záznamu