@article{29d74edd2e6f4582ba47fe4dadf2d9e8,
title = "Two-sided ubiquitin binding explains specificity of the TAB2 NZF domain",
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.",
author = "Yogesh Kulathu and Masato Akutsu and Anja Bremm and Kay Hofmann and David Komander",
note = "Funding Information: We would like to thank P. Cohen (Medical Research Council Protein Phosphorylation Unit), H. Scheel (Miltenyi Biotec), D.Veprintsev,A. Pobbati, R.Williams, O. Perisic, F. Gorrec,Y.Ye (Medical Research Council Laboratory of Molecular Biology) for help and reagents.Y.K., M.A. and A.B. are Medical Research Council Career Development Fellows.",
year = "2009",
month = dec,
doi = "10.1038/nsmb.1731",
language = "English",
volume = "16",
pages = "1328--1330",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "Nature Publishing Group",
number = "12",
}