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- W2070010982 abstract "Most of the actions of 1,25-dihydroxyvitamin D 3 [1,25(OH) 2 D 3 ] are mediated by binding to the Vitamin D nuclear receptor (VDR). The crystal structure of a deletion mutant (Δ165-215) of the VDR ligand-binding domain (LBD) bound to 1,25(OH) 2 D 3 indicates that amino acid residues tyrosine-143 and serine-278 form hydrogen bonding interactions with the 3-hydroxyl group of 1,25(OH) 2 D 3 . Studies of VDR and three mutants (Y143F, S278A, and Y143F/S278A) did not indicate any differences in the binding affinity between the variant receptors and the wild-type receptor. This might indicate that the 3-hydroxyl group binds differently to the full-length VDR than the to deletion mutant. To further investigate, four deletion VDR mutants were constructed: VDR Δ165-215 , VDR Δ165-215 (Y143F), VDR Δ165-215 (S278A), VDR Δ165-215 (Y143F/S278A). There were no significant differences in binding affinity between the wild-type receptor and the deletion mutants except for VDR Δ165-215 (Y143F/S278A). In gene activation assays, VDR constructs with the single mutation Y143F and the double mutation Y143F/S278A, but not the single mutation S278A required higher doses of 1,25(OH) 2 D 3 for half-maximal response. This suggests that there are some minor structural and functional differences between the wild-type VDR and the Δ165-215 deletion mutant and that Y143 residue is more important for receptor function than residue S278." @default.
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- W2070010982 date "2004-05-01" @default.
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- W2070010982 title "Role of residues 143 and 278 of the human nuclear Vitamin D receptor in the full-length and Δ165-215 deletion mutant" @default.
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- W2070010982 doi "https://doi.org/10.1016/j.jsbmb.2004.03.051" @default.
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