Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 23, Issue 15, Pages -Publisher
MDPI
DOI: 10.3390/ijms23158445
Keywords
structure function relationship; vitamin D; rare diseases
Funding
- Agence Nationale de la Recherche [ANR-13-BSV8-0024-01, ANR-19-CE17-0006-01, ANR-21-CE17-0009]
- Fondation pour la Recherche Medicale [FRM-FDT20140930978]
- IdEx Unistra [ANR-10-IDEX-0002]
- SFRI-STRAT'US project [ANR 20-SFRI-0012]
- EUR IMCBio [ANR-17-EURE-0023]
- Agence Nationale de la Recherche (ANR) [ANR-21-CE17-0009, ANR-19-CE17-0006] Funding Source: Agence Nationale de la Recherche (ANR)
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This study demonstrates that BXL-62 and Gemini-72, two C-20-modified vitamin D analogs, restore the transcriptional activities of VDR variants unresponsive to the natural ligand. The elucidated mechanisms of action highlight the mutual adaptation between the ligand and the VDR ligand-binding pocket.
The Vitamin D receptor (VDR) plays a key role in calcium homeostasis, as well as in cell proliferation and differentiation. Among the large number of VDR ligands that have been developed, we have previously shown that BXL-62 and Gemini-72, two C-20-modified vitamin D analogs are highly potent VDR agonists. In this study, we show that both VDR ligands restore the transcriptional activities of VDR variants unresponsive to the natural ligand and identified in patients with rickets. The elucidated mechanisms of action underlying the activities of these C-20-modified analogs emphasize the mutual adaptation of the ligand and the VDR ligand-binding pocket.
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