2f1x

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[[Image:2f1x.gif|left|200px]]
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{{Structure
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{{STRUCTURE_2f1x| PDB=2f1x | SCENE= }}
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|RELATEDENTRY=[[2f1w|2F1W]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1x OCA], [http://www.ebi.ac.uk/pdbsum/2f1x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f1x RCSB]</span>
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'''Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a p53 peptide'''
'''Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a p53 peptide'''
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[[Category: Jeffrey, P D.]]
[[Category: Jeffrey, P D.]]
[[Category: Shi, Y.]]
[[Category: Shi, Y.]]
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[[Category: hausp]]
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[[Category: Hausp]]
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[[Category: p53 recognition]]
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[[Category: P53 recognition]]
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[[Category: peptide binding]]
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[[Category: Peptide binding]]
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[[Category: substrate recognition]]
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[[Category: Substrate recognition]]
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[[Category: traf-like domain]]
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[[Category: Traf-like domain]]
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[[Category: ubp]]
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Revision as of 00:21, 4 May 2008

Image:2f1x.gif

Template:STRUCTURE 2f1x

Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a p53 peptide


Overview

Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7), a deubiquitylating enzyme of the ubiquitin-specific processing protease family, specifically deubiquitylates both p53 and MDM2, hence playing an important yet enigmatic role in the p53-MDM2 pathway. Here we demonstrate that both p53 and MDM2 specifically recognize the N-terminal tumor necrosis factor-receptor associated factor (TRAF)-like domain of HAUSP in a mutually exclusive manner. HAUSP preferentially forms a stable HAUSP-MDM2 complex even in the presence of excess p53. The HAUSP-binding elements were mapped to a peptide fragment in the carboxy-terminus of p53 and to a short-peptide region preceding the acidic domain of MDM2. The crystal structures of the HAUSP TRAF-like domain in complex with p53 and MDM2 peptides, determined at 2.3-A and 1.7-A resolutions, respectively, reveal that the MDM2 peptide recognizes the same surface groove in HAUSP as that recognized by p53 but mediates more extensive interactions. Structural comparison led to the identification of a consensus peptide-recognition sequence by HAUSP. These results, together with the structure of a combined substrate-binding-and-deubiquitylation domain of HAUSP, provide important insights into regulation of the p53-MDM2 pathway by HAUSP.

About this Structure

2F1X is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway., Hu M, Gu L, Li M, Jeffrey PD, Gu W, Shi Y, PLoS Biol. 2006 Feb;4(2):e27. Epub 2006 Jan 17. PMID:16402859 Page seeded by OCA on Sun May 4 03:21:57 2008

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