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| {{STRUCTURE_1yze| PDB=1yze | SCENE= }} | | {{STRUCTURE_1yze| PDB=1yze | SCENE= }} |
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| '''Crystal structure of the N-terminal domain of USP7/HAUSP.'''
| | ===Crystal structure of the N-terminal domain of USP7/HAUSP.=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15808506}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15808506 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15808506}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Deubiquitinating enzyme]] | | [[Category: Deubiquitinating enzyme]] |
| [[Category: Traf domain]] | | [[Category: Traf domain]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:59:56 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:57:50 2008'' |