期刊
EMBO JOURNAL
卷 28, 期 24, 页码 3903-3909出版社
WILEY
DOI: 10.1038/emboj.2009.345
关键词
crystallography; NF-kappa B; ubiquitin; zinc finger
资金
- JSPS
- Grants-in-Aid for Scientific Research [21687009] Funding Source: KAKEN
TAB2 and TAB3 activate the Jun N-terminal kinase and nuclear factor-kappa B 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 angstrom 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. The EMBO Journal (2009) 28, 3903-3909. doi: 10.1038/emboj.2009.345; Published online 19 November 2009
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