2f1z

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[[Image:2f1z.gif|left|200px]]
[[Image:2f1z.gif|left|200px]]
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{{Structure
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|PDB= 2f1z |SIZE=350|CAPTION= <scene name='initialview01'>2f1z</scene>, resolution 3.2&Aring;
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The line below this paragraph, containing "STRUCTURE_2f1z", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitin_thiolesterase Ubiquitin thiolesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.15 3.1.2.15] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= USP7, HAUSP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_2f1z| PDB=2f1z | SCENE= }}
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|RELATEDENTRY=[[2f1w|2F1W]], [[2f1x|2F1X]], [[2f1y|2F1Y]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1z OCA], [http://www.ebi.ac.uk/pdbsum/2f1z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f1z RCSB]</span>
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'''Crystal structure of HAUSP'''
'''Crystal structure of HAUSP'''
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[[Category: Jeffrey, P D.]]
[[Category: Jeffrey, P D.]]
[[Category: Shi, Y.]]
[[Category: Shi, Y.]]
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[[Category: deubiquitinating enzyme]]
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[[Category: Deubiquitinating enzyme]]
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[[Category: hausp]]
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[[Category: Hausp]]
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[[Category: substrate recognition]]
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[[Category: Substrate recognition]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:22:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:56:48 2008''
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Revision as of 00:22, 4 May 2008

Image:2f1z.gif

Template:STRUCTURE 2f1z

Crystal structure of HAUSP


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

2F1Z 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 03:22:01 2008

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