3VT8: Crystal Structures Of Rat Vdr-lbd With W282r Mutation

The vitamin D receptor (VDR), a member of the nuclear receptor superfamily, functions as a ligand-dependent transcription factor for various genes. Hereditary vitamin D-resistant rickets (HVDRR), an autosomal recessive disease, is caused by mutations in the VDR. In particular, the missense mutations R274L and W286R in the ligand-binding domain of the VDR can severely reduce or even eliminate natural hormone responsiveness. Here, we report a crystal structure analysis of the R270L and W282R mutants of rat VDR (human R274L and W286R, respectively) in complex with the natural hormone and synthetic ligands. We also studied the folding properties of the mutant proteins by using circular dichroism spectra. Our study indicates that these mutations result in only local structural modifications. We discuss why these mutations disrupt the VDR function and provide clues to develop effective ligands for the treatment of HVDRR.
PDB ID: 3VT8Download
MMDB ID: 110211
PDB Deposition Date: 2012/5/19
Updated in MMDB: 2013/09
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
synthetic construct
Similar Structures:
Biological Unit for 3VT8: monomeric; determined by author
Molecular Components in 3VT8
Label Count Molecule
Protein (1 molecule)
Vitamin D3 Receptor(Gene symbol: Vdr)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

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