3W0I

Crystal Structure of Rat VDR Ligand Binding Domain in Complex with Novel Nonsecosteroidal Ligands

3W0I の概要

• エントリーDOI: 10.2210/pdb3w0i/pdb
• 関連するPDBエントリー: 3W0G 3W0H 3W0J
• 分子名称: Vitamin D3 Receptor, Mediator of RNA polymerase II transcription subunit 1, (2S)-3-{4-[3-(4-{[(2R)-2-hydroxy-3,3-dimethylbutyl]oxy}phenyl)pentan-3-yl]phenoxy}propane-1,2-diol, ... (4 entities in total)
• 機能のキーワード: gene regulation, 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: 30756.50

構造登録者

Shimizu, T.,Asano, L.,Kuwabara, N.,Ito, I.,Waku, T.,Yanagisawa, J.,Miyachi, H. (登録日: 2012-10-30, 公開日: 2013-10-09, 最終更新日: 2023-11-08)

主引用文献

Asano, L.,Ito, I.,Kuwabara, N.,Waku, T.,Yanagisawa, J.,Miyachi, H.,Shimizu, T.
Structural basis for vitamin D receptor agonism by novel non-secosteroidal ligands.
Febs Lett., 587:957-963, 2013

PubMed Abstract: Non-secosteroidal ligands for vitamin D receptor (VDR) have been developed for the agonist with non-calcemic profiles. Here, we provide the structural mechanism of VDR agonism by novel non-secosteroidal ligands. All ligands had the similar efficacy, while two had the higher potency. Crystallographic analyses revealed that all ligands interacted with helix H10 and the loop between helices H6 and H7 in a similar manner, but also that the two ligands with higher potency had different interaction modes. This study suggests that distinct ligand potency depend upon differences in the formation and rearrangement of hydrogen-bond networks induced by each ligand.

PubMed: 23462137
DOI: 10.1016/j.febslet.2013.02.028

実験手法

X-RAY DIFFRACTION (1.9 Å)