[Characterization of ligand-dependent transactivation regions of the human vitamin D receptor].
The 1,25-dihydroxyvitamin D receptor (VDR) belongs to the nuclear hormone receptor family. Mutational analysis revealed that the carboxyl-terminal region between leucine-417 and glutamic acid-420 of the human VDR is essential for the ligand-dependent transactivation. Mutant VDR at this AF-2 region exhibits only weak suppressive effect on the transactivation via the wild type receptor compared to the estrogen and vitamin A receptors, which confer the strong dominant negative effect. Using the AF-2 mutant VDR protein, we demonstrated a 65kD nuclear protein, which binds to the AF-2 region of the human VDR in a ligand dependent manner.
Department of Pediatrics, Osaka University School of Medicine.
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Nakajima
D005786:Gene Expression Regulation; D006801:Humans; D008024:Ligands; D009154:Mutation; D009687:Nuclear Proteins / Q000235:genetics / Q000502:physiology; D011485:Protein Binding; D018167:Receptors, Calcitriol / Q000737:chemistry / Q000235:genetics* / Q000502:physiology; D015533:Transcriptional Activation
D008024:Ligands; D009687:Nuclear Proteins; D018167:Receptors, Calcitriol