Abstract
The vitamin D receptor (VDR) and its natural ligand, 1α,25-dihydroxyvitamin D3 (1,25(OH)2D3, or calcitriol), regulate mineral homeostasis and metabolism, cell growth, differentiation, antiproliferation, apoptosis, and adaptive/innate immune responses. VDR is widely expressed in various tissues and represents an important therapeutic target in the treatment of diverse disorders. VDR mediates the biological effects of its ligand by regulating the transcription of target genes. Because of the high pharmaceutical potential of VDR ligands, numerous 1,25(OH)2D3 analogs have been synthesized to selectively modulate receptor activity. Their mechanism of action have been intensively investigated, and structural details of the VDR signaling are now available for various VDR ligands that comprise secosteroidal synthetic analogs and 1,25(OH)2D3 mimics with scaffold structurally unrelated to 1,25(OH)2D3. The crystal structures demonstrate and explain ligand-binding mode and mutual ligand–protein adaptability: VDR can accommodate various analogs as long as the length of the ligand and the hydrogen bonds are maintained. Structural studies correlate structural features and the mechanism of ligand action at the level of atomic interactions with the receptor. Furthermore, the activity of several VDR ligands have been improved based on structural analysis, demonstrating the importance of such studies.
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