2fop: Difference between revisions

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[[Image:2fop.gif|left|200px]]<br /><applet load="2fop" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2fop.gif|left|200px]]
caption="2fop, resolution 2.10&Aring;" />
 
'''The Crystal Strucure of the N-terminal domain of HAUSP/USP7 complexed with mdm2 peptide 147-150'''<br />
{{Structure
|PDB= 2fop |SIZE=350|CAPTION= <scene name='initialview01'>2fop</scene>, resolution 2.10&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [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]
|GENE= HAUSP, USP7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''The Crystal Strucure of the N-terminal domain of HAUSP/USP7 complexed with mdm2 peptide 147-150'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2FOP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FOP OCA].  
2FOP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FOP OCA].  


==Reference==
==Reference==
Molecular recognition of p53 and MDM2 by USP7/HAUSP., Sheng Y, Saridakis V, Sarkari F, Duan S, Wu T, Arrowsmith CH, Frappier L, Nat Struct Mol Biol. 2006 Mar;13(3):285-91. Epub 2006 Feb 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16474402 16474402]
Molecular recognition of p53 and MDM2 by USP7/HAUSP., Sheng Y, Saridakis V, Sarkari F, Duan S, Wu T, Arrowsmith CH, Frappier L, Nat Struct Mol Biol. 2006 Mar;13(3):285-91. Epub 2006 Feb 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16474402 16474402]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: math domain]]
[[Category: math domain]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:33 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:54:58 2008''

Revision as of 17:55, 20 March 2008

File:2fop.gif


PDB ID 2fop

Drag the structure with the mouse to rotate
, resolution 2.10Å
Gene: HAUSP, USP7 (Homo sapiens)
Activity: Ubiquitin thiolesterase, with EC number 3.1.2.15
Coordinates: save as pdb, mmCIF, xml



The Crystal Strucure of the N-terminal domain of HAUSP/USP7 complexed with mdm2 peptide 147-150


OverviewOverview

The ubiquitin-specific protease, USP7, has key roles in the p53 pathway whereby it stabilizes both p53 and MDM2. We show that the N-terminal domain of USP7 binds two closely spaced 4-residue sites in both p53 and MDM2, falling between p53 residues 359-367 and MDM2 residues 147-159. Cocrystal structures with USP7 were determined for both p53 peptides and for one MDM2 peptide. These peptides bind the same surface of USP7 as Epstein-Barr nuclear antigen-1, explaining the competitive nature of the interactions. The structures and mutagenesis data indicate a preference for a P/AXXS motif in peptides that bind USP7. Contacts made by serine are identical and crucial for all peptides, and Trp165 in the peptide-binding pocket of USP7 is also crucial. These results help to elucidate the mechanism of substrate recognition by USP7 and the regulation of the p53 pathway.

About this StructureAbout this Structure

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

ReferenceReference

Molecular recognition of p53 and MDM2 by USP7/HAUSP., Sheng Y, Saridakis V, Sarkari F, Duan S, Wu T, Arrowsmith CH, Frappier L, Nat Struct Mol Biol. 2006 Mar;13(3):285-91. Epub 2006 Feb 12. PMID:16474402

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