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7E62

Mouse TAB2 NZF in complex with Lys6-linked diubiquitin

Summary for 7E62
Entry DOI10.2210/pdb7e62/pdb
Descriptorubiquitin, Ubiquitin, TGF-beta-activated kinase 1 and MAP3K7-binding protein 2, ... (6 entities in total)
Functional Keywordsubiquitin, protein binding
Biological sourceMus musculus (Mouse)
More
Total number of polymer chains6
Total formula weight47352.58
Authors
Sato, Y.,Li, Y.,Okatsu, K.,Fukai, S. (deposition date: 2021-02-21, release date: 2021-08-18, Last modification date: 2023-11-29)
Primary citationLi, Y.,Okatsu, K.,Fukai, S.,Sato, Y.
Structural basis for specific recognition of K6-linked polyubiquitin chains by the TAB2 NZF domain.
Biophys.J., 120:3355-3362, 2021
Cited by
PubMed Abstract: TAK1-binding protein 2 (TAB2) has generally been considered to bind specifically to K63-linked polyubiquitin chains via its C-terminal Npl4 zinc-finger (NZF) domain. However, a recent study showed that the NZF domain of TAB2 (TAB2-NZF) could also interact with K6-linked polyubiquitin chains. Here, we report the crystal structure of TAB2-NZF in complex with K6-linked diubiquitin (K6-Ub) at 1.99-Å resolution. TAB2-NZF simultaneously interacts with the distal and proximal ubiquitin moieties of K6-Ub. By comparing the structures of TAB2-NZF in complex with K6-Ub and with K63-linked diubiquitin (K63-Ub), we reveal that the binding mechanism of TAB2-NZF with K6-Ub is similar to that with K63-Ub, except for the flexible C-terminal region of the distal ubiquitin. Therefore, we conclude that the C-terminal flexibility of the distal ubiquitin contributes to the dual specificity of TAB2-NZF toward K6- and K63-linked ubiquitin chains. This study provides important insights into the functions of K6-linked ubiquitin chains, which are currently unclear.
PubMed: 34242591
DOI: 10.1016/j.bpj.2021.06.037
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.99 Å)
Structure validation

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数据于2025-12-03公开中

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