ArticleJournal of lipid research2013
Crystal structures of complexes of vitamin D receptor ligand-binding domain with lithocholic acid derivatives.
Article in Journal of lipid research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 41 citations in OpenAlex.
- The Pathological Effects of Circulating Hydrophobic Bile Acids in Alzheimer's Disease.Journal of Alzheimer's disease reports · 2023Review
- Oligoarginine-Conjugated Peptide Foldamers Inhibiting Vitamin D Receptor-Mediated Transcription.ACS omega · 2022Article
- The Role of CYP3A in Health and Disease.Biomedicines · 2022Review
- Lithocholic Acid Amides as Potent Vitamin D Receptor Agonists.Biomolecules · 2022Article
- The bridge of the gut-joint axis: Gut microbial metabolites in rheumatoid arthritis.Frontiers in immunology · 2022Review
- Physiological Role of Bile Acids Modified by the Gut Microbiome.Microorganisms · 2021Review
- The Physiological Importance of Bile Acid Structure and Composition on Glucose Homeostasis.Current diabetes reports · 2020Review
- Vitamin D and Its Synthetic Analogs.Journal of medicinal chemistry · 2019Review
- The Biosynthesis, Signaling, and Neurological Functions of Bile Acids.Biomolecules · 2019Review
- Parallel Chemistry Approach to Identify Novel Nuclear Receptor Ligands Based on the GW0742 Scaffold.ACS combinatorial science · 2017Article
- Endogenously produced nonclassical vitamin D hydroxy-metabolites act as "biased" agonists on VDR and inverse agonists on RORα and RORγ.The Journal of steroid biochemistry and molecular biology · 2017Review
- Synthesis and evaluation of vitamin D receptor-mediated activities of cholesterol and vitamin D metabolites.European journal of medicinal chemistry · 2016Article
- Evolutionary and Functional Diversification of the Vitamin D Receptor-Lithocholic Acid Partnership.PloS one · 2016Article
- Relationship between Structure and Conformational Change of the Vitamin D Receptor Ligand Binding Domain in 1α,25-Dihydroxyvitamin D3 Signaling.Molecules (Basel, Switzerland) · 2015Review
- Functional diversification of vitamin D receptor paralogs in teleost fish after a whole genome duplication event.Endocrinology · 2014Article
- Structural considerations of vitamin D signaling.Frontiers in physiology · 2014Review
- Nuclear Receptors in Drug Metabolism, Drug Response and Drug Interactions.Nuclear receptor researchArticle
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The secondary bile acid lithocholic acid (LCA) and its derivatives act as selective modulators of the vitamin D receptor (VDR), although their structures fundamentally differ from that of the natural hormone 1α,25-dihydroxyvitamin D3 [1,25(OH)2D3)]. Here, we have determined the crystal structures of the ligand-binding domain of rat VDR (VDR-LBD) in ternary complexes with a synthetic partial peptide of the coactivator MED1 (mediator of RNA polymerase II transcription subunit 1) and four ligands, LCA, 3-keto LCA, LCA acetate, and LCA propionate, with the goal of elucidating their agonistic mechanism. LCA and its derivatives bind to the same ligand-binding pocket (LBP) of VDR-LBD that 1,25(OH)2D3 binds to, but in the opposite orientation; their A-ring is positioned at the top of the LBP, whereas their acyclic tail is located at the bottom of the LBP. However, most of the hydrophobic and hydrophilic interactions observed in the complex with 1,25(OH)2D3 are reproduced in the complexes with LCA and its derivatives. Additional interactions between VDR-LBD and the C-3 substituents of the A-ring are also observed in the complexes with LCA and its derivatives. These may result in the observed difference in the potency among the LCA-type ligands.
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