3AUN

Crystal structure of the rat vitamin D receptor ligand binding domain complexed with YR335 and a synthetic peptide containing the NR2 box of DRIP 205

3AUN の概要

• エントリーDOI: 10.2210/pdb3aun/pdb
• 関連するPDBエントリー: 2ZFX
• 分子名称: Vitamin D3 receptor, DRIP 205 NR2 box peptide, (2R)-2-{4-[3-(4-{[(2R)-2-hydroxy-3,3-dimethylbutyl]oxy}-3-methylphenyl)pentan-3-yl]-2-methylphenoxy}butane-1,4-diol, ... (4 entities in total)
• 機能のキーワード: binding sites, biphenyl compounds, protein binding, tertiary, rats, receptors, calcitriol, vitamin d, transcription
• 由来する生物種: Rattus norvegicus (rat); 詳細
• 細胞内の位置: Nucleus: P13053 Q15648
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32099.05

構造登録者

Kakuda, S.,Takimoto-Kamimura, M. (登録日: 2011-02-10, 公開日: 2012-02-15, 最終更新日: 2023-11-01)

主引用文献

Demizu, Y.,Takahashi, T.,Kaneko, F.,Sato, Y.,Okuda, H.,Ochiai, E.,Horie, K.,Takagi, K.,Kakuda, S.,Takimoto-Kamimura, M.,Kurihara, M.
Design, synthesis and X-ray crystallographic study of new nonsecosteroidal vitamin D receptor ligands
Bioorg.Med.Chem.Lett., 21:6104-6107, 2011

PubMed Abstract: We designed and synthesized nonsecosteroidal vitamin D receptor (VDR) ligands that formed H-bonds with six amino acid residues (Tyr143, Ser233, Arg270, Ser274, His301 and His393) of the VDR ligand-binding domain. The ligand YR335 exhibited potent transcriptional activity, which was comparable to those of 1α,25-dihydroxyvitamin D(3) and YR301. The crystal structure of the complex formed between YR335 and the VDR ligand-binding domain was solved, which revealed that YR335 formed H-bonds with the six amino acid residues mentioned above.

PubMed: 21889334
DOI: 10.1016/j.bmcl.2011.08.047

実験手法

X-RAY DIFFRACTION (1.81 Å)