Summary
PDB 3M7R deposited: 2010-03-17 modified: 2010-05-05
Title Crystal structure of VDR H305Q mutant
Authors Hourai, S., Moras, D., Rochel, N.
Method X-RAY DIFFRACTION
Structure factors resolution 1.8 rfactor 0.211 rfree 0.241
DPI 0.33 theoretical min: 0.15
Citations

In the nuclear receptor of vitamin D (VDR) histidine 305 participates to the anchoring of the ligand. The VDR H305Q mutation was identified in a patient who exhibited the hereditary vitamin D-resistant rickets (HVDRR). We report the crystal structure of human VDR H305Q-ligand binding domain bound to 1alpha,25(OH)2D3 solved at 1.8A resolution. The protein adopts the active conformation of the wild-type liganded VDR. A local conformational flexibility at the mutation site weakens the hydrogen bond between the 25-OH with Gln305, thus explaining the lower affinity of the mutant proteins for calcitriol. The structure provides the basis for a rational approach to the design of more potent ligands for the treatment of HVDRR.

J Steroid Biochem Mol Biol. 2010 Jul;121(1-2):84-7. Epub 2010 Apr 18.

Cross References
Database source Identifier Description
PubMed 20403435 JSBBEZ
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
3M7R/0 3M7R 0 monomer 0 1 1 2005