Putative helices 3 and 5 of the human vitamin D3 receptor are important for the binding of calcitriol

FEBS Letters

Mäenpää, Pekka H¹  Väisänen, Sami¹  Rouvinen, Juha² 

[1] Department of Biochemistry and Biotechnology, University of Kuopio, P.O. Box 1627, FIN-70211 Kuopio, Finland;Department of Chemistry, University of Joensuu, P.O. Box 111, FIN-80101 Joensuu, Finland

关键词: Vitamin D receptor;    Ligand binding;    Site-directed mutagenesis;    Conformation;    Calcitriol;    1α;    25-dihydroxyvitamin D3;    hER;    human estrogen receptor;    LBD;    ligand binding domain;    MC1288;    20-epi-1α;    25-dihydroxyvitamin D3;    hPR;    human progesterone receptor;    hRARγ;    human retinoic acid receptor-γ;    hRXRα;    human retinoid X receptor-α;    rTRα;    rat thyroid hormone receptor-α;    hVDR;    human vitamin D receptor;   

DOI  :  10.1016/S0014-5793(98)01436-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown