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http://purl.uniprot.org/citations/16474402http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16474402http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16474402http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.org/dc/terms/identifier"doi:10.1038/nsmb1067"xsd:string
http://purl.uniprot.org/citations/16474402http://purl.org/dc/terms/identifier"doi:10.1038/nsmb1067"xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Arrowsmith C.H."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Arrowsmith C.H."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Frappier L."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Frappier L."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Duan S."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Duan S."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Sheng Y."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Sheng Y."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Wu T."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Wu T."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Saridakis V."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Saridakis V."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Sarkari F."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/author"Sarkari F."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/name"Nat. Struct. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/pages"285-291"xsd:string
http://purl.uniprot.org/citations/16474402http://purl.uniprot.org/core/pages"285-291"xsd:string