3A9J

Crystal structure of the mouse TAB2-NZF in complex with Lys63-linked di-ubiquitin

3A9J の概要

• エントリーDOI: 10.2210/pdb3a9j/pdb
• 関連するPDBエントリー: 3A9K
• 分子名称: Ubiquitin, Mitogen-activated protein kinase kinase kinase 7-interacting protein 2, ZINC ION, ... (5 entities in total)
• 機能のキーワード: protein complex, cytoplasm, isopeptide bond, metal-binding, zinc, zinc-finger, signaling protein-metal binding protein complex, signaling protein/metal binding protein
• 由来する生物種: Mus musculus (mouse); 詳細
• 細胞内の位置: Nucleus : Q99K90
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 21224.64

構造登録者

Sato, Y.,Yoshikawa, A.,Yamashita, M.,Yamagata, A.,Fukai, S. (登録日: 2009-10-29, 公開日: 2009-12-08, 最終更新日: 2024-10-30)

主引用文献

Sato, Y.,Yoshikawa, A.,Yamashita, M.,Yamagata, A.,Fukai, S.
Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by NZF domains of TAB2 and TAB3
Embo J., 28:3903-3909, 2009

PubMed Abstract: TAB2 and TAB3 activate the Jun N-terminal kinase and nuclear factor-kappaB pathways through the specific recognition of Lys 63-linked polyubiquitin chains by its Npl4 zinc-finger (NZF) domain. Here we report crystal structures of the TAB2 and TAB3 NZF domains in complex with Lys 63-linked diubiquitin at 1.18 and 1.40 A resolutions, respectively. Both NZF domains bind to the distal ubiquitin through a conserved Thr-Phe dipeptide that has been shown to be important for the interaction of the NZF domain of Npl4 with monoubiquitin. In contrast, a surface specific to TAB2 and TAB3 binds the proximal ubiquitin. Both the distal and proximal binding sites of the TAB2 and TAB3 NZF domains recognize the Ile 44-centred hydrophobic patch on ubiquitin but do not interact with the Lys 63-linked isopeptide bond. Mutagenesis experiments show that both binding sites are required to enable binding of Lys 63-linked diubiquitin. We therefore propose a mechanism for the recognition of Lys 63-linked polyubiquitin chains by TAB2 and TAB3 NZF domains in which diubiquitin units are specifically recognized by a single NZF domain.

PubMed: 19927120
DOI: 10.1038/emboj.2009.345

実験手法

X-RAY DIFFRACTION (1.18 Å)