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Titolo:
Three-dimensional modeling of and ligand docking to vitamin D receptor ligand binding domain
Autore:
Yamamoto, K; Masuno, H; Choi, M; Nakashima, K; Taga, T; Ooizumi, H; Umesono, K; Sicinska, W; VanHooke, J; DeLuca, HF; Yamada, S;
Indirizzi:
Tokyo Med & Dent Univ, Inst Biomat & Bioengn, Chiyoda Ku, Tokyo 1010062, Japan Tokyo Med & Dent Univ Tokyo Japan 1010062 iyoda Ku, Tokyo 1010062, Japan Tokyo Med & Dent Univ, Med Res Inst, Chiyoda Ku, Tokyo 1010062, Japan Tokyo Med & Dent Univ Tokyo Japan 1010062 iyoda Ku, Tokyo 1010062, Japan Kyoto Univ, Dept Genet & Mol Biol, Kyoto 6068507, Japan Kyoto Univ KyotoJapan 6068507 pt Genet & Mol Biol, Kyoto 6068507, Japan Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA Univ Wisconsin Madison WI USA 53706 , Dept Biochem, Madison, WI 53706 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 4, volume: 97, anno: 2000,
pagine: 1467 - 1472
SICI:
0027-8424(20000215)97:4<1467:TMOALD>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
THYROID-HORMONE RECEPTOR; SIDE-CHAIN CONFORMATION; CRYSTAL-STRUCTURE; 1-ALPHA,25-DIHYDROXYVITAMIN D-3; RETINOIC ACID; RAR-GAMMA; NUCLEAR; ANALOGS; SUPERFAMILY; ANTAGONISM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Yamada, S Tokyo Med & Dent Univ, Inst Biomat & Bioengn, Chiyoda Ku, 2-3-10SurugadaiKanda, Tokyo 1010062, Japan Tokyo Med & Dent Univ 2-3-10 Surugadai Kanda Tokyo Japan 1010062
Citazione:
K. Yamamoto et al., "Three-dimensional modeling of and ligand docking to vitamin D receptor ligand binding domain", P NAS US, 97(4), 2000, pp. 1467-1472

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 1 alpha,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). Threeresidues forming hydrogen bonds with the functionally important 1 alpha- and 25-hydroxyl groups of 1 alpha,25-dihydroxyvitamin D-3 were identified and confirmed by mutational analysis: the 1 alpha-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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 12:00:30