ArticleProceedings of the National Academy of Sciences of the United States of America2001
Crystal structures of the vitamin D receptor complexed to superagonist 20-epi ligands.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- An extension of jamdock-suite for virtual screening from raw chemical datasets.STAR protocols · 2026Article
- Vitamin D receptor signaling in inflammatory senescence-associated skin aging: Mechanisms and therapeutic potentials.Journal of cell communication and signaling · 2026Article
- Modulation of the vitamin D receptor by traditional Chinese medicines and bioactive compounds: potential therapeutic applications in VDR-dependent diseases.Frontiers in pharmacology · 2024Review
- The Influence of Single Nucleotide Polymorphisms on Vitamin D Receptor Protein Levels and Function in Chronic Liver Disease.International journal of molecular sciences · 2023Article
- Vitamin D Analogs Bearing C-20 Modifications Stabilize the Agonistic Conformation of Non-Responsive Vitamin D Receptor Variants.International journal of molecular sciences · 2022Article
- In Silico Prediction of the Metabolic Resistance of Vitamin D Analogs against CYP3A4 Metabolizing Enzyme.International journal of molecular sciences · 2022Article
- Gene-Regulatory Potential of 25-Hydroxyvitamin DFrontiers in nutrition · 2022Article
- PSNtools for standalone and web-based structure network analyses of conformational ensembles.Computational and structural biotechnology journal · 2022Article
- New Approaches to Assess Mechanisms of Action of Selective Vitamin D Analogues.International journal of molecular sciences · 2021Review
- Transcriptome-Wide Profile of 25-Hydroxyvitamin DNutrients · 2021Article
- Design, Synthesis, Evaluation and Structure of Allenic 1α,25-Dihydroxyvitamin DChemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Endocrine disruption of vitamin D activity by perfluoro-octanoic acid (PFOA).Scientific reports · 2020Article
- webPSN v2.0: a webserver to infer fingerprints of structural communication in biomacromolecules.Nucleic acids research · 2020Article
- Computational Analysis of Crystallization Additives for the Identification of New Allosteric Sites.ACS omega · 2020Article
- Vitamin D and Its Synthetic Analogs.Journal of medicinal chemistry · 2019Review
- Vitamins D: Relationship between Structure and Biological Activity.International journal of molecular sciences · 2018Review
- Functional analyses of a novel missense and other mutations of the vitamin D receptor in association with alopecia.Scientific reports · 2017Article
- Vitamin D: Metabolism, Molecular Mechanism of Action, and Pleiotropic Effects.Physiological reviews · 2016Review
- Relationship between Structure and Conformational Change of the Vitamin D Receptor Ligand Binding Domain in 1α,25-Dihydroxyvitamin D3 Signaling.Molecules (Basel, Switzerland) · 2015Review
- Vitamin D metabolism, mechanism of action, and clinical applications.Chemistry & biology · 2014Review
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5 authors.
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Abstract
The crystal structures of the ligand-binding domain (LBD) of the vitamin D receptor complexed to 1alpha,25(OH)(2)D(3) and the 20-epi analogs, MC1288 and KH1060, show that the protein conformation is identical, conferring a general character to the observation first made for retinoic acid receptor (RAR) that, for a given LBD, the agonist conformation is unique, the ligands adapting to the binding pocket. In all complexes, the A- to D-ring moieties of the ligands adopt the same conformation and form identical contacts with the protein. Differences are observed only for the 17beta-aliphatic chains that adapt their conformation to anchor the 25-hydroxyl group to His-305 and His-397. The inverted geometry of the C20 methyl group induces different paths of the aliphatic chains. The ligands exhibit a low-energy conformation for MC1288 and a more strained conformation for the two others. KH1060 compensates this energy cost by additional contacts. Based on the present data, the explanation of the superagonist effect is to be found in higher stability and longer half-life of the active complex, thereby excluding different conformations of the ligand binding domain.
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