7E62
Mouse TAB2 NZF in complex with Lys6-linked diubiquitin
Summary for 7E62
| Entry DOI | 10.2210/pdb7e62/pdb |
| Descriptor | ubiquitin, Ubiquitin, TGF-beta-activated kinase 1 and MAP3K7-binding protein 2, ... (6 entities in total) |
| Functional Keywords | ubiquitin, protein binding |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 6 |
| Total formula weight | 47352.58 |
| 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 citation | Li, 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: 34242591DOI: 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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