Putative helices 3 and 5 of the human vitamin D3 receptor are important for the binding of calcitriol.
We have introduced eleven point mutations into the human vitamin D receptor by site-directed mutagenesis in order to identify some of the amino acid residues that are important for ligand binding. The amino acid residues Ser225, His229, Asp232, Val234, Ser235, Tyr236, Ser237, Lys240, Ile242, Lys246 (helix 3), and Ser275 (helix 5) of the human vitamin D receptor were substituted by alanine. We report here that His229, Asp232, and Ser237 have an important role in the binding of calcitriol. In addition, the amino acid residues Tyr236 and Ser275 also seem to participate in the ligand binding process.
Väisänen
S
S
Department of Biochemistry and Biotechnology, University of Kuopio, Finland. vaisanen@messi.uku.fi
Rouvinen
J
J
Mäenpää
P H
PH
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001665:Binding Sites; D002117:Calcitriol / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017354:Point Mutation; D014176:Protein Biosynthesis; D017510:Protein Folding; D017433:Protein Structure, Secondary; D018167:Receptors, Calcitriol / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism
D008024:Ligands; D018167:Receptors, Calcitriol; D014357:Trypsin; D002117:Calcitriol