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2f1y

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[[Image:2f1y.gif|left|200px]]
[[Image:2f1y.gif|left|200px]]
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{{Structure
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{{STRUCTURE_2f1y| PDB=2f1y | SCENE= }}
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|RELATEDENTRY=[[2f1w|2F1W]], [[2f1x|2F1X]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f1y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1y OCA], [http://www.ebi.ac.uk/pdbsum/2f1y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f1y RCSB]</span>
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'''Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a MDM2 peptide'''
'''Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a MDM2 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: mdm2]]
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[[Category: Mdm2]]
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[[Category: mdm2 recognition]]
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[[Category: Mdm2 recognition]]
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[[Category: substrate binding]]
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[[Category: Substrate binding]]
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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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[[Category: Ubp]]
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[[Category: usp7]]
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[[Category: Usp7]]
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Revision as of 00:22, 4 May 2008

Image:2f1y.gif

Template:STRUCTURE 2f1y

Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a MDM2 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

2F1Y 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 03:22:00 2008

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