Crystallographic Studies of Retinoid Complexes with Plasma Retinol-Binding Protein

Three-dimensional structures of complexes between bovine plasma retinol-binding protein and three retinol analogs have been determined to 1.8-1.9-Å resolution. The dataset, authored by Giuseppe Zanotti from the University of Padua, models the binding of fenretinide, all-trans retinoic acid, and axerophthene, revealing conformational changes in the protein loop region.

Use Cases

• Analyzing protein conformational changes based on the described loop region flexibility upon ligand binding.
• Comparing ligand binding affinity based on the described steric hindrance and hydroxyl group presence.
• Modeling protein-ligand docking based on the described beta-barrel cavity and retinol analog conformations.
• Studying the interaction between retinol-binding protein and transthyretin based on the described affinity changes for different retinoid complexes.

Strengths

• High-resolution structural data determined to 1.8-1.9 Å.
• Direct comparison of three specific retinol analogs (fenretinide, all-trans retinoic acid, axerophthene) with retinol.
• Quantitative root mean square deviation values (0.17 to 0.24 Å) provided for structural similarity.

Limitations

• Row count is unknown, which may limit suitability assessment.
• Column-level documentation is absent; field semantics must be inferred after download.
• Last update date is unknown; freshness unverified.

Provenance

Source

University of Padua

Collection Method

Crystallographic studies, likely from X-ray diffraction.