NMR STRUCTURE OF HOLO CELLULAR RETINOL-BINDING PROTEIN II

Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics.

The Structure and Dynamics of Rat Apo-Cellular Retinol-Binding Protein II in Solution: Comparison with the X-ray Structure

Crystal Structures of Holo and Apo-Cellular Retinol-Binding Protein II

Lipid-Binding Proteins: A Family of Fatty Acid and Retinoid Transport Proteins

The NMR Solution Structure of Intestinal Fatty Acid-Binding Protein Complexed with Palmitate: Application of a Novel Distance Geometry Algorithm

Ligand Binding Alters the Backbone Mobility of Intestinal Fatty Acid-Binding Protein as Monitored by 15N NMR Relaxation and 1H Exchange

NMR STRUCTURE OF APO CELLULAR RETINOL-BINDING PROTEIN II

The structure was determined using triple-resonance NMR spectroscopy

FINAL PENALTY FUNCTION VALUES WITHIN 2 STANDARD DEVIATIONS FROM THE MEAN

The structure calculations were carried out using TINKER, a software package for molecular mechanics and dynamics. The protocol employs metric matrix distance geometry with pairwise Gaussian metrization followed by simulated annealing. The unique distance geometry algorithm implemented in TINKER overcomes the sampling and scaling problems of earlier distance geometry methods and is computationally more efficient.

1.5 mM CELLULAR RETINOL-BINDING PROTEIN II U-15N,13C, complexed with all-trans retinol in 1-to-1 molar ratio; 20 mM phosphate buffer

1.5 mM CELLULAR RETINOL-BINDING PROTEIN II U-15N, complexed with all-trans retinol in 1-to-1 molar ratio; 20 mM phosphate buffer

0.2 mM CELLULAR RETINOL-BINDING PROTEIN II natural abundance, complexed with (2,3,6,7,8,9,10,11,19-13C)-all-trans retinol in 1-to-1 molar ratio; 20 mM phosphate buffer

PROTEIN-LIGAND COMPLEX, BETA BARREL, HELIX-TURN-HELIX, TRANSPORT PROTEIN