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Updated: Aug 7, 2026

Quantitative Analysis of Dietary Vitamin A Metabolites in Murine Ocular and Non-Ocular Tissues Using High-Performance Liquid Chromatography
Published on: December 27, 2024
Ligand binding domain of vitamin D receptors
1Département de Biologie et de Génomique Structurales, IGBMC, CNRS/INSERM/Université Louis Pasteur, Parc d'Innovation BP10142, 67404 Illkirch cedex, France.
Abstract:
The vitamin D receptor, a member of the nuclear receptor subgroup NR1I, is regulated by 1alpha,25(OH)2D3 to control calcium metabolism, cell proliferation and differentiation and immunomodulation. The therapeutic applications of vitamin D metabolites are wide. To develop efficient therapy, the elucidation of the structure-function relationships of VDR and its ligands are essential. In this review we will focus on the current structural understanding of the interactions of ligands in the ligand binding pocket of the VDR. These structures revealed the mutual adaptability of the ligands and the protein. In silico modeling has further revealed a possible new pocket in the VDR LBD responsible of the non-genomic action mediated by VDR. With the availability of all these structural information on VDR LBD, new ligands that are more selective, such as non-steroidal ligands, could be designed by taking into account the flexibility of some VDR regions. Tissue selectivity may also be achieved by developing ligands that specifically activate the non-genomic pathway.
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