2vfj | pdb_00002vfj
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STRUCTURE OF THE A20 OVARIAN TUMOUR (OTU) DOMAIN
Overview
The NF-kappaB regulator A20 antagonises IKK activation by modulating, Lys63-linked polyubiquitination of cytokine receptor associated factors, including TRAF2/6 and RIP1. Here we describe the crystal structure of the, N-terminal Ovarian Tumour (OTU) 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. Biochemical analysis shows a preference of, the isolated A20 OTU domain for Lys48-linked tetraubiquitin in vitro, suggesting that additional specificity factors might be required for the, physiological function of A20 in cells.
About this Structure
2VFJ is a Single protein structure of sequence from Homo sapiens with SO4 and MG as ligands. Active as Ubiquitinyl hydrolase 1, with EC number 3.4.19.12 Known structural/functional Sites: AC1, AC2, AC3, AC4 and AC5. Full crystallographic information is available from OCA.
Reference
Structure of the A20 OTU domain and mechanistic insights into deubiquitination., Komander D, Barford D, Biochem J. 2007 Oct 26;. PMID:17961127
Page seeded by OCA on Wed Jan 23 11:53:28 2008
Proteopedia Page Contributors and Editors (what is this?)
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- Homo sapiens
- Single protein
- Ubiquitinyl hydrolase 1
- Barford, D.
- Komander, D.
- MG
- SO4
- Apoptosis
- Cysteine protease
- Cytokine signalling
- Cytoplasm
- Deubiquitinating enzyme
- Dna-binding
- Hydrolase
- Lys63- linked
- Metal-binding
- Nf-kb
- Nucleus
- Otu
- Ovarian tumour
- Phosphorylation
- Polymorphism
- Protease
- Thiol protease
- Ubiquitin
- Ubl conjugation pathway
- Zinc
- Zinc-finger
