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- W2016245743 abstract "Fragment molecular orbital–interfragment interaction energy calculations of the vitamin D receptor (VDR)/1α,25-dihydroxyvitamin D3 complex were utilized to assign functions of key residues of the VDR. Only one residue forms a significant interaction with the corresponding hydroxy group of the ligand, although two residues are located around each hydroxy group. The degradation of binding affinity for derivatives upon removal of a hydroxy group is closely related to the trend in the strength of the hydrogen bonds. Type II hereditary rickets due to an Arg274 point mutation is caused by the lack of the strongest hydrogen bond." @default.
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- W2016245743 date "2006-03-01" @default.
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- W2016245743 title "Functions of key residues in the ligand-binding pocket of vitamin D receptor: Fragment molecular orbital–interfragment interaction energy analysis" @default.
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- W2016245743 doi "https://doi.org/10.1016/j.cplett.2005.12.078" @default.
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