| http://purl.uniprot.org/citations/24098653 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24098653 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/24098653 | http://www.w3.org/2000/01/rdf-schema#comment | "Src homology 2 (SH2) domains play a critical role in cellular signal transduction. They bind to peptides containing phosphotyrosine (pY) with various specificities that depend on the flanking amino-acid residues. The SH2 domain of growth-factor receptor-bound protein 2 (Grb2) specifically recognizes pY-X-N-X, whereas the SH2 domains in phosphatidylinositol 3-kinase (PI3K) recognize pY-X-X-M. Binding of the pY site in CD28 (pY-M-N-M) by PI3K and Grb2 through their SH2 domains is a key step that triggers the CD28 signal transduction for T cell activation and differentiation. In this study, we determined the crystal structure of the Grb2 SH2 domain in complex with a pY-containing peptide derived from CD28 at 1.35 Å resolution. The peptide was found to adopt a twisted U-type conformation, similar to, but distinct from type-I β-turn. In all previously reported crystal structures, the peptide bound to the Grb2 SH2 domains adopts a type-I β-turn conformation, except those with a proline residue at the pY+3 position. Molecular modeling also suggests that the same peptide bound to PI3K might adopt a very different conformation."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0074482"xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.pone.0074482"xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Abe R."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Abe R."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Morii H."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Morii H."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Ito N."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Ito N."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Takahashi J."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Takahashi J."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Higo K."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Higo K."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Ikura T."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Ikura T."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Oda M."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/author | "Oda M."xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/name | "PLoS ONE"xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/name | "PLoS ONE"xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/pages | "E74482"xsd:string |
| http://purl.uniprot.org/citations/24098653 | http://purl.uniprot.org/core/pages | "E74482"xsd:string |