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• W2007203425 abstract "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 1α,25(OH)2D3 solved at 1.8 Å 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." @default.
• W2007203425 created "2016-06-24" @default.
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• W2007203425 creator A5048176888 @default.
• W2007203425 creator A5048793419 @default.
• W2007203425 date "2010-07-01" @default.
• W2007203425 modified "2023-09-27" @default.
• W2007203425 title "Crystal structure of hereditary vitamin D-resistant rickets—Associated mutant H305Q of vitamin D nuclear receptor bound to its natural ligand" @default.
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• W2007203425 doi "https://doi.org/10.1016/j.jsbmb.2010.04.008" @default.
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