Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 16, Issue 12, Pages 1328-1330Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1731
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Funding
- Medical Research Council [MC_U105192732] Funding Source: Medline
- MRC [MC_U105192732] Funding Source: UKRI
- Medical Research Council [MC_U105192732] Funding Source: researchfish
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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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