2foo: Difference between revisions

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[[Image:2foo.gif|left|200px]]<br />

[[Image:2foo.gif|left|200px]]<br /><applet load="2foo" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="2foo" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="2foo, resolution 2.20Å" />

'''The Crystal Strucure of the N-terminal domain of HAUSP/USP7 complexed with p53 peptide 359-362'''<br />

==Overview==

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.

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 Structure==

2FOO 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=2FOO OCA].

2FOO 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=2FOO OCA].

==Reference==

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[[Category: Single protein]]

[[Category: Ubiquitin thiolesterase]]

[[Category: Arrowsmith, C.H.]]

[[Category: Arrowsmith, C H.]]

[[Category: Duan, S.]]

[[Category: Frappier, L.]]

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[[Category: math domain]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 22~~:08:~~30 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:38 2008''

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@@ Line 1: / Line 1: @@
-[[Image:2foo.gif|left|200px]]<br />
+[[Image:2foo.gif|left|200px]]<br /><applet load="2foo" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="2foo" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="2foo, resolution 2.20&Aring;" />
 '''The Crystal Strucure of the N-terminal domain of HAUSP/USP7 complexed with p53 peptide 359-362'''<br />
 ==Overview==
-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.
+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 Structure==
-FOO 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FOO OCA].
+FOO 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=2FOO OCA].
 ==Reference==
@@ Line 15: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Ubiquitin thiolesterase]]
-[[Category: Arrowsmith, C.H.]]
+[[Category: Arrowsmith, C H.]]
 [[Category: Duan, S.]]
 [[Category: Frappier, L.]]
@@ Line 24: / Line 23: @@
 [[Category: math domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:08:30 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:38 2008''