Cell Reports volume 3, issue 3, P747-758 2013 DOI: 10.1016/j.celrep.2013.01.033 View full text
Daqi Tu, Zehua Zhu, Alicia Y. Zhou, Cai-hong Yun, Kyung-Eun Lee, Angela V. Toms, Yiqun Li, Gavin P. Dunn, Edmond Chan, Tran Thai, Shenghong Yang, Scott B. Ficarro, Jarrod A. Marto, Hyesung Jeon et al.

Abstract: Summary Upon stimulation by pathogen-associated inflammatory signals, the atypical IκB kinase TBK1 induces type-I interferon expression and modulates NF-κB signaling. Here we describe the 2.4 Å-resolution crystal structure of nearly full-length TBK1 in complex with specific inhibitors. The structure reveals a novel dimeric assembly, created by an extensive network of interactions among the kinase, ubiquitin-like (ULD) and scaffold/dimerization (SDD) domains. An intact TBK1 dimer undergoes K63-linked polyubiqu…

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