1yy6

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Revision as of 18:20, 12 November 2007

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spinqualitylabelsall models 1yy6, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

The Crystal Strucure of the N-terminal domain of HAUSP/USP7 complexed with an EBNA1 peptide

Overview

USP7/HAUSP is a key regulator of p53 and Mdm2 and is targeted by the, Epstein-Barr nuclear antigen 1 (EBNA1) protein of Epstein-Barr virus, (EBV). We have determined the crystal structure of the p53 binding domain, of USP7 alone and bound to an EBNA1 peptide. This domain is an, eight-stranded beta sandwich similar to the TRAF-C domains of TNF-receptor, associated factors, although the mode of peptide binding differs, significantly from previously observed TRAF-peptide interactions in the, sequence (DPGEGPS) and the conformation of the bound peptide. NMR chemical, shift analyses of USP7 bound by EBNA1 and p53 indicated that p53 binds the, same pocket as EBNA1 but makes less extensive contacts with USP7., Functional studies indicated that EBNA1 binding to USP7 can protect cells, from apoptotic challenge by lowering p53 levels. The data provide a, structural and conceptual framework for understanding how EBNA1 might, contribute to the survival of Epstein-Barr virus-infected cells.

About this Structure

1YY6 is a Single protein structure of sequence from Homo sapiens with NA as ligand. Active as Ubiquitin thiolesterase, with EC number 3.1.2.15 Full crystallographic information is available from OCA.

Reference

Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization., Saridakis V, Sheng Y, Sarkari F, Holowaty MN, Shire K, Nguyen T, Zhang RG, Liao J, Lee W, Edwards AM, Arrowsmith CH, Frappier L, Mol Cell. 2005 Apr 1;18(1):25-36. PMID:15808506

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