2MBH

NMR structure of EKLF(22-40)/Ubiquitin Complex

2MBH の概要

• エントリーDOI: 10.2210/pdb2mbh/pdb
• NMR情報: BMRB: 19399
• 分子名称: Krueppel-like factor 1, Ubiquitin (2 entities in total)
• 機能のキーワード: protein-protein complex, eklf, ubiquitin, uim/miu, transcription factor tad, transcription
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: Q13351
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13020.64

構造登録者

Raiola, L.,Omichinski, J.G. (登録日: 2013-07-31, 公開日: 2013-10-09, 最終更新日: 2024-05-15)

主引用文献

Raiola, L.,Lussier-Price, M.,Gagnon, D.,Lafrance-Vanasse, J.,Mascle, X.,Arseneault, G.,Legault, P.,Archambault, J.,Omichinski, J.G.
Structural Characterization of a Noncovalent Complex between Ubiquitin and the Transactivation Domain of the Erythroid-Specific Factor EKLF.
Structure, 21:2014-2024, 2013

PubMed Abstract: Like other acidic transactivation domains (TAD), the minimal TAD from the erythroid-specific transcription factor EKLF (EKLFTAD) has been shown to contribute both to its transcriptional activity as well as to its ubiquitin(UBI)-mediated degradation. In this article, we examine the activation-degradation role of the acidic TAD of EKLF and demonstrate that the first 40 residues (EKLFTAD1) within this region form a noncovalent interaction with UBI. Nuclear magnetic resonance (NMR) structural studies of an EKLFTAD1-UBI complex show that EKLFTAD1 adopts a 14-residue α helix that forms the recognition interface with UBI in a similar manner as the UBI-interacting helix of Rabex5. We also identify a similar interaction between UBI and the activation-degradation region of SREBP1a, but not with the activation-degradation regions of p53, GAL4, and VP16. These results suggest that select activation-degradation regions like the ones found in EKLF and SREBP1a function in part through their ability to form noncovalent interactions with UBI.

PubMed: 24139988
DOI: 10.1016/j.str.2013.08.027

実験手法

SOLUTION NMR