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

Kulathu Y, Akutsu M, Bremm A, Hofmann K, Komander D
Nat Struct Mol Biol 16 1328-30 (2009)
Related entries: 2wx0, 2wx1

Cited: 135 times
EuropePMC logo PMID: 19935683

Abstract

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.

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