5DAD

Crystal Structure of Human KEAP1 BTB Domain in Complex with Small Molecule TX64014

5DAD の概要

• エントリーDOI: 10.2210/pdb5dad/pdb
• 関連するPDBエントリー: 5DAF
• 分子名称: Kelch-like ECH-associated protein 1, (6aS,7S,10aS)-8-hydroxy-4-methoxy-2,7,10a-trimethyl-5,6,6a,7,10,10a-hexahydrobenzo[h]quinazoline-9-carbonitrile (3 entities in total)
• 機能のキーワード: keap1, trascription regulation, btb domain, cysteine modification, c1-(r)-cys151 adduct, transcription
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cytoplasm: Q14145
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15894.32

構造登録者

Huerta, C.,Jiang, X.,Trevino, I.,Bender, C.F.,Swinger, K.K.,Stoll, V.S.,Ferguson, D.A.,Thomas, P.J.,Probst, B.,Dulubova, I.,Visnick, M.,Wigley, W.C. (登録日: 2015-08-19, 公開日: 2016-08-10, 最終更新日: 2024-11-13)

主引用文献

Huerta, C.,Jiang, X.,Trevino, I.,Bender, C.F.,Ferguson, D.A.,Probst, B.,Swinger, K.K.,Stoll, V.S.,Thomas, P.J.,Dulubova, I.,Visnick, M.,Wigley, W.C.
Characterization of novel small-molecule NRF2 activators: Structural and biochemical validation of stereospecific KEAP1 binding.
Biochim.Biophys.Acta, 1860:2537-2552, 2016

PubMed Abstract: Semi-synthetic oleanane triterpenoid antioxidant inflammation modulators (tpAIMs) are small molecules that interact with KEAP1 cysteine residue 151 (C151) and activate NRF2. Exploration of the structure-activity relationship between the tpAIMs and KEAP1 is limited by the predominantly hydrocarbon nature of the oleanane triterpenoid pentacyclic ring structure. Therefore, we used novel, chemically-tractable, synthetic antioxidant inflammation modulators (sAIMs) to probe the stereoselectivity of the ligand-protein interaction.

PubMed: 27474998
DOI: 10.1016/j.bbagen.2016.07.026

実験手法

X-RAY DIFFRACTION (2.61 Å)