2WX1
TAB2 NZF DOMAIN IN COMPLEX WITH Lys63-linked tri-ubiquitin, P212121
Summary for 2WX1
Entry DOI | 10.2210/pdb2wx1/pdb |
Related | 1AAR 1E0Q 1P3Q 1UZX 1V80 1V81 1WR6 1WRD 1YD8 2C7M 2C7N 2D3G 2FID 2FIF 2WWZ 2WX0 |
Descriptor | UBIQUITIN, MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7-INTERACTING PROTEIN 2, ZINC ION (3 entities in total) |
Functional Keywords | protein binding, isopeptide bond, nzf domain, zinc-finger, metal-binding |
Biological source | HOMO SAPIENS More |
Cellular location | Membrane; Peripheral membrane protein: Q9NYJ8 |
Total number of polymer chains | 3 |
Total formula weight | 20845.18 |
Authors | Kulathu, Y.,Akutsu, M.,Bremm, A.,Hofmann, K.,Komander, D. (deposition date: 2009-10-30, release date: 2009-11-24, Last modification date: 2024-10-09) |
Primary citation | Kulathu, Y.,Akutsu, M.,Bremm, A.,Hofmann, K.,Komander, D. Two-Sided Ubiquitin Binding Explains Specificity of the Tab2 Nzf Domain Nat.Struct.Mol.Biol., 16:1328-, 2009 Cited by PubMed 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. PubMed: 19935683DOI: 10.1038/NSMB.1731 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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