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http://purl.uniprot.org/citations/18941216http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18941216http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18941216http://www.w3.org/2000/01/rdf-schema#comment"T cells are known to cross-react with diverse peptide MHC Ags through their alphabeta TCR. To explore the basis of such cross-reactivity, we examined the 2C TCR that recognizes two structurally distinct ligands, SIY-K(b) and alloantigen QL9-L(d). In this study we characterized the cross-reactivity of several high-affinity 2C TCR variants that contained mutations only in the CDR3alpha loop. Two of the TCR lost their ability to cross-react with the reciprocal ligand (SIY-K(b)), whereas another TCR (m67) maintained reactivity with both ligands. Crystal structures of four of the TCRs in complex with QL9-L(d) showed that CDR1, CDR2, and CDR3beta conformations and docking orientations were remarkably similar. Although the CDR3alpha loop of TCR m67 conferred a 2000-fold higher affinity for SIY-K(b), the TCR maintained the same docking angle on QL9-L(d) as the 2C TCR. Thus, CDR3alpha dictated the affinity and level of cross-reactivity, yet it did so without affecting the conserved docking orientation."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.org/dc/terms/identifier"doi:10.4049/jimmunol.181.9.6255"xsd:string
http://purl.uniprot.org/citations/18941216http://purl.org/dc/terms/identifier"doi:10.4049/jimmunol.181.9.6255"xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/author"Garcia K.C."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/author"Garcia K.C."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/author"Kranz D.M."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/author"Kranz D.M."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/author"Colf L.A."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/author"Colf L.A."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/author"Jones L.L."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/author"Jones L.L."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/author"Stone J.D."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/author"Stone J.D."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/name"J. Immunol."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/name"J Immunol"xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/pages"6255-6264"xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/pages"6255-6264"xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/title"Distinct CDR3 conformations in TCRs determine the level of cross-reactivity for diverse antigens, but not the docking orientation."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/title"Distinct CDR3 conformations in TCRs determine the level of cross-reactivity for diverse antigens, but not the docking orientation."xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/volume"181"xsd:string
http://purl.uniprot.org/citations/18941216http://purl.uniprot.org/core/volume"181"xsd:string