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• W2076172803 abstract "We present a new method to investigate the details of interaction between vitamin D nuclear receptor (VDR) and various ligands, namely a two-dimensional alanine scanning mutational analysis. In this method, the transactivation of various ligands is studied in conjunction with a series of alanine scanning mutations of the residues lining the ligand binding pocket (LBP) of VDR, and the complete set of results is profiled in a patch table. We investigated examples from four structurally diverse groups of known VDR ligands: the native vitamin D hormone and two compounds with the same side chain configuration; four 20-epi compounds; three 19-nor compounds; and two nonsecosteroids. The patch table of the results indicates characteristics of each group in terms of its interaction with 18 LBP residues. We demonstrate the validity of this approach by application to docking studies of the two nonsecosteroids." @default.
• W2076172803 created "2016-06-24" @default.
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• W2076172803 date "2003-03-01" @default.
• W2076172803 modified "2023-10-11" @default.
• W2076172803 title "Interaction between Vitamin D Receptor and Vitamin D Ligands" @default.
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• W2076172803 doi "https://doi.org/10.1016/s1074-5521(03)00050-4" @default.
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