ReviewMolecules (Basel, Switzerland)2015
Relationship of structure and function of DNA-binding domain in vitamin D receptor.
Review in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- A case of vitamin D-dependent rickets type 2A presenting with hypophosphatemia without hypocalcemia.JCEM case reports · 2026Article
- Genetics and Vitamin D Interactions in Osteoporosis: A Path to Precision Medicine.Journal of cellular and molecular medicine · 2025Review
- VDR and deubiquitination control neuronal oxidative stress and microglial inflammation in Parkinson's disease.Cell death discovery · 2024Article
- Dissection of an impact of VDR and RXRA on the genomic activity of 1,25(OH)Molecular and cellular endocrinology · 2024Article
- Article
- Interplay between Vitamin D and Sphingolipids in Cardiometabolic Diseases.International journal of molecular sciences · 2023Review
- The Role of Zinc in Bone Tissue Health and Regeneration-a Review.Biological trace element research · 2023Review
- Modulation of the vitamin D/vitamin D receptor system in osteoporosis pathogenesis: insights and therapeutic approaches.Journal of orthopaedic surgery and research · 2023Review
- Quercetin activates vitamin D receptor and ameliorates breast cancer induced hepatic inflammation and fibrosis.Frontiers in nutrition · 2023Article
- Vitamin D receptor (BsmI) gene polymorphism and allele frequency among chronic kidney disease patients in south Indian population.Bioinformation · 2023Article
- Zinc and its role in vitamin D function.Current research in physiology · 2022Review
- An Update on Vitamin D Metabolism.International journal of molecular sciences · 2020Review
- Vitamin D receptor targets hepatocyte nuclear factor 4α and mediates protective effects of vitamin D in nonalcoholic fatty liver disease.The Journal of biological chemistry · 2020Article
- Vitamin D: Newer Concepts of Its Metabolism and Function at the Basic and Clinical Level.Journal of the Endocrine Society · 2020Article
- Genetic Causes of Rickets.Journal of clinical research in pediatric endocrinology · 2017Review
- HDX reveals the conformational dynamics of DNA sequence specific VDR co-activator interactions.Nature communications · 2017Article
- Intestinal toxicity of the type B trichothecene mycotoxin fusarenon-X: whole transcriptome profiling reveals new signaling pathways.Scientific reports · 2017Article
- Low back pain and FokI (rs2228570) polymorphism of vitamin D receptor in athletes.BMC sports science, medicine & rehabilitation · 2017Article
- THE INVOLVEMENT OF VDR PROMOTER METHYLATION, CDX-2 VDR POLYMORPHISM AND VITAMIN D LEVELS IN MALE INFERTILITY.Acta endocrinologica (Bucharest, Romania : 2005)Article
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5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While the structure of the DNA-binding domain (DBD) of the vitamin D receptor (VDR) has been determined in great detail, the roles of its domains and how to bind the motif of its target genes are still under debate. The VDR DBD consists of two zinc finger modules and a C-terminal extension (CTE), at the end of the C-terminal of each structure presenting α-helix. For the first zinc finger structure, N37 and S-box take part in forming a dimer with 9-cis retinoid X receptor (RXR), while V26, R50, P-box and S-box participate in binding with VDR response elements (VDRE). For the second zinc finger structure, P61, F62 and H75 are essential in the structure of the VDR homodimer with the residues N37, E92 and F93 of the downstream of partner VDR, which form the inter-DBD interface. T-box of the CTE, especially the F93 and I94, plays a critical role in heterodimerization and heterodimers-VDRE binding. Six essential residues (R102, K103, M106, I107, K109, and R110) of the CTE α-helix of VDR construct one interaction face, which packs against the DBD core of the adjacent symmetry mate. In 1,25(OH)2D3-activated signaling, the VDR-RXR heterodimer may bind to DR3-type VDRE and ER9-type VDREs of its target gene directly resulting in transactivation and also bind to DR3-liked nVDRE of its target gene directly resulting in transrepression. Except for this, 1α,25(OH)2D3 ligand VDR-RXR may bind to 1αnVDRE indirectly through VDIR, resulting in transrepression of the target gene. Upon binding of 1α,25(OH)2D3, VDR can transactivate and transrepress its target genes depending on the DNA motif that DBD binds.
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