Differential binding of retinol analogs to two homologous cellular retinol-binding proteins.
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.
Rong
D
D
Department of Medicine, Washington University, St. Louis, Missouri 63110.
Lovey
A J
AJ
Rosenberger
M
M
d'Avignon
A
A
Ponder
J
J
Li
E
E
D000818:Animals; D001059:Apoproteins / Q000378:metabolism; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008968:Molecular Conformation; D051381:Rats; D011994:Recombinant Proteins / Q000378:metabolism; D012177:Retinol-Binding Proteins / Q000378:metabolism*; D054840:Retinol-Binding Proteins, Cellular; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity; D014801:Vitamin A / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism*
D001059:Apoproteins; D007202:Indicators and Reagents; D011994:Recombinant Proteins; D012177:Retinol-Binding Proteins; D054840:Retinol-Binding Proteins, Cellular; D014801:Vitamin A