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http://purl.uniprot.org/citations/10488331http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10488331http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10488331http://www.w3.org/2000/01/rdf-schema#comment"We have solved the high-resolution X-ray structure of 14-3-3 bound to two different phosphoserine peptides, representing alternative substrate-binding motifs. These structures reveal an evolutionarily conserved network of peptide-protein interactions within all 14-3-3 isotypes, explain both binding motifs, and identify a novel intrachain phosphorylation-mediated loop structure in one of the peptides. A 14-3-3 mutation disrupting Raf signaling alters the ligand-binding cleft, selecting a different phosphopeptide-binding motif and different substrates than the wild-type protein. Many 14-3-3: peptide contacts involve a C-terminal amphipathic alpha helix containing a putative nuclear export signal, implicating this segment in both ligand and Crm1 binding. Structural homology between the 14-3-3 NES structure and those within I kappa B alpha and p53 reveals a conserved topology recognized by the Crm1 nuclear export machinery."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)80363-9"xsd:string
http://purl.uniprot.org/citations/10488331http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)80363-9"xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Budman J."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Budman J."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Cantley L.C."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Cantley L.C."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Gamblin S.J."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Gamblin S.J."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Rittinger K."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Rittinger K."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Xu J."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Xu J."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Smerdon S.J."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Smerdon S.J."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Volinia S."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Volinia S."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Yaffe M.B."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/author"Yaffe M.B."xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/10488331http://purl.uniprot.org/core/name"Mol. Cell"xsd:string