Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2WX1

TAB2 NZF DOMAIN IN COMPLEX WITH Lys63-linked tri-ubiquitin, P212121

Summary for 2WX1
Entry DOI10.2210/pdb2wx1/pdb
Related1AAR 1E0Q 1P3Q 1UZX 1V80 1V81 1WR6 1WRD 1YD8 2C7M 2C7N 2D3G 2FID 2FIF 2WWZ 2WX0
DescriptorUBIQUITIN, MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 7-INTERACTING PROTEIN 2, ZINC ION (3 entities in total)
Functional Keywordsprotein binding, isopeptide bond, nzf domain, zinc-finger, metal-binding
Biological sourceHOMO SAPIENS
More
Cellular locationMembrane; Peripheral membrane protein: Q9NYJ8
Total number of polymer chains3
Total formula weight20845.18
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 citationKulathu, 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: 19935683
DOI: 10.1038/NSMB.1731
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

226707

数据于2024-10-30公开中

PDB statisticsPDBj update infoContact PDBjnumon