1U6D

Crystal structure of the Kelch domain of human Keap1

1U6D の概要

• エントリーDOI: 10.2210/pdb1u6d/pdb
• 分子名称: kelch-like ECH-associated protein 1 (2 entities in total)
• 機能のキーワード: beta-propeller, kelch repeat motif, protein binding
• 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: 33694.53

構造登録者

Li, X.,Zhang, D.,Hannink, M.,Beamer, L.J. (登録日: 2004-07-29, 公開日: 2004-10-12, 最終更新日: 2024-02-14)

主引用文献

Li, X.,Zhang, D.,Hannink, M.,Beamer, L.J.
Crystal structure of the kelch domain of human keap1
J.Biol.Chem., 279:54750-54758, 2004

PubMed Abstract: Keap1 is a substrate adaptor protein for an ubiquitin ligase complex that targets the Nrf2 transcription factor for degradation. Keap1 binds Nrf2 through its C-terminal Kelch domain, which contains six copies of the evolutionarily conserved kelch repeat sequence motif. The structure of the Kelch domain from human Keap1 has been determined by x-ray crystallography to a resolution of 1.85 A. The Kelch domain forms a 6-bladed beta-propeller structure, with residues at the C terminus forming the first strand in the first blade. Key structural roles have been identified for the highly conserved glycine, tyrosine, and tryptophan residues that define the kelch repeat sequence motif. In addition, we show that substitution of a single amino acid located within a loop that extends out from the bottom of the beta-propeller structure abolishes binding of Nrf2. The structure of the Kelch domain of Keap1 represents a high quality model for the superfamily of eukaryotic kelch repeat proteins and provides insight into how disease-causing mutations perturb the structural integrity of the Kelch domain.

PubMed: 15475350
DOI: 10.1074/jbc.M410073200

実験手法

X-RAY DIFFRACTION (1.85 Å)