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Three-dimensional modeling of and ligand docking to vitamin D receptor ligand binding domain.

ABSTRACT: The ligand binding domain of the human vitamin D receptor (VDR) was modeled based on the crystal structure of the retinoic acid receptor. The ligand binding pocket of our VDR model is spacious at the helix 11 site and confined at the beta-turn site. The ligand 1alpha, 25-dihydroxyvitamin D(3) was assumed to be anchored in the ligand binding pocket with its side chain heading to helix 11 (site 2) and the A-ring toward the beta-turn (site 1). Three residues forming hydrogen bonds with the functionally important 1alpha- and 25-hydroxyl groups of 1alpha,25-dihydroxyvitamin D(3) were identified and confirmed by mutational analysis: the 1alpha-hydroxyl group is forming pincer-type hydrogen bonds with S237 and R274 and the 25-hydroxyl group is interacting with H397. Docking potential for various ligands to the VDR model was examined, and the results are in good agreement with our previous three-dimensional structure-function theory.

SUBMITTER: Yamamoto K 

PROVIDER: S-EPMC26457 | biostudies-literature | 2000 Feb

REPOSITORIES: biostudies-literature

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Three-dimensional modeling of and ligand docking to vitamin D receptor ligand binding domain.

Yamamoto K K   Masuno H H   Choi M M   Nakashima K K   Taga T T   Ooizumi H H   Umesono K K   Sicinska W W   VanHooke J J   DeLuca H F HF   Yamada S S  

Proceedings of the National Academy of Sciences of the United States of America 20000201 4

The ligand binding domain of the human vitamin D receptor (VDR) was modeled based on the crystal structure of the retinoic acid receptor. The ligand binding pocket of our VDR model is spacious at the helix 11 site and confined at the beta-turn site. The ligand 1alpha, 25-dihydroxyvitamin D(3) was assumed to be anchored in the ligand binding pocket with its side chain heading to helix 11 (site 2) and the A-ring toward the beta-turn (site 1). Three residues forming hydrogen bonds with the function  ...[more]

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