Journal
BIOCHEMICAL JOURNAL
Volume 409, Issue -, Pages 77-85Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20071399
Keywords
A20 binding inhibitor of NF-kappa B (ABIN); cytokine signalling; deubiquitinating enzyme; inhibitor of kappa B kinase (IKK); Lys(63)-linked ubiquitin; nuclear factor kappa B (NF-kappa B); TGF (transforming growth factor)-beta-activated kinase (TAK1); tumour-necrosis-factor-receptor-associated factor (TRAF)
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The NF-kappa B (nuclear factor kappa B) regulator A20 antagonises IKK [I kappa B (inhibitor of kappa B) kinase] activation by modulating Lys(63)-linked polyubiquitination of cytokine-receptor-associated factors including TRAF2/6 (tumour-necrosis-factor-receptor-associated factor 2/6) and RIP] (receptor-interacting protein 1). In the present paper we describe the crystal structure of the N-terminal OTU (ovarian tumour) deubiquitinase domain of A20, which differs from other deubiquitinases but shares the minimal catalytic core with otubain-2. Analysis of conserved surface regions allows prediction of ubiquitin-binding sites for the proximal and distal ubiquitin molecules. Structural and biochemical analysis suggests a novel architecture of the catalytic triad, which might be present in a subset of OTU domains including Cezanne and TRABID (TRAF-binding domain). Biochemical analysis shows a preference of the isolated A20 OTU domain for Lys(48)-linked tetraubiquitin in vitro suggesting that additional specificity factors might be required for the physiological function of A20 in cells.
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