The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand.

@article{Rochel2000TheCS,
  title={The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand.},
  author={Natacha Rochel and Jean Marie Wurtz and André Mitschler and Bruno P. Klaholz and Dino Moras},
  journal={Molecular cell},
  year={2000},
  volume={5 1},
  pages={
          173-9
        }
}

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In the present study recombinant human nuclear VDR and its ligand binding domain (LBD) were expressed in Spodoptera frugiperda insect cells and in E.coli cells and their biochemical and biophysical properties were purified.

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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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Biological activity assays, structural analysis, and molecular dynamics simulations indicate that the recognition of two ligand molecules is crucial for VDR agonism by LCA, and the unique binding mode of LCA provides clues for the development of new chemical compounds that target alternative binding sites for therapeutic applications.

Vitamin D and Its Receptor from a Structural Perspective

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An overview of the current knowledge of VDR structures is provided and the recent progress in understanding the complex mechanism of action of 1,25D3 from a structural perspective is explored.

Crystal structures of complexes of vitamin D receptor ligand-binding domain with lithocholic acid derivatives

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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 and four ligands, LCA, 3-keto LCA), LCA acetate, and LCA propionate are determined with the goal of elucidating their agonistic mechanism.

Structurally and functionally important amino acids of the agonistic conformation of the human vitamin D receptor.

TLDR
The results suggest that structurally different agonists have distinct ligand-receptor interactions and that the amino acid residues H229, D232, E269, F279, and Y295 are critical for the agonistic conformation of the VDR.
...

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