Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain

Yogesh Kulathu, Masato Akutsu, Anja Bremm, Kay Hofmann, David Komander

研究成果: Article査読

147 被引用数 (Scopus)

抄録

The protein kinase TAK1 is activated by binding to Lys63 (K63)-linked ubiquitin chains through its subunit TAB2. Here we analyze crystal structures of the TAB2 NZF domain bound to Lys63-linked di-and triubiquitin, revealing that TAB2 binds adjacent ubiquitin moieties via two distinct binding sites. The conformational constraints imposed by TAB2 on a Lys63 dimer cannot be adopted by linear chains, explaining why TAK1 cannot be activated by linear ubiquitination events.

本文言語English
ページ(範囲)1328-1330
ページ数3
ジャーナルNature Structural and Molecular Biology
16
12
DOI
出版ステータスPublished - 2009 12月
外部発表はい

ASJC Scopus subject areas

  • 構造生物学
  • 分子生物学

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