2vfj

From Proteopedia

---

Revision as of 09:53, 23 January 2008

proteopedia linkproteopedia link

spinqualitylabelsall models 2vfj, resolution 3.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 and as ligands. Active as Ubiquitinyl hydrolase 1, with EC number 3.4.19.12 Known structural/functional Sites: , , , and . 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