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http://purl.uniprot.org/citations/15131131http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15131131http://www.w3.org/2000/01/rdf-schema#comment"Mutational studies of T cell receptor (TCR) contact residues on the surface of the human class I major histocompatibility complex (MHC) molecule HLA-A2 have identified a "functional hot spot" that comprises Arg(65) and Lys(66) and is involved in recognition by most peptide-specific HLA-A2-restricted TCRs. Although there is a significant amount of functional data on the effects of mutations at these positions, there is comparatively little biochemical information that could illuminate their mode of action. Here, we have used a combination of fluorescence anisotropy, functional assays, and Biacore binding experiments to examine the effects of mutations at these positions on the peptide-MHC interaction and TCR recognition. The results indicate that mutations at both position 65 and position 66 influence peptide binding by HLA-A2 to various extents. In particular, mutations at position 66 result in significantly increased peptide dissociation rates. However, these effects are independent of their effects on TCR recognition, and the Arg(65)-Lys(66) region thus represents a true "hot spot" for TCR recognition. We also made the observation that in vitro T cell reactivity does not scale with the half-life of the peptide-MHC complex, as is often assumed. Finally, position 66 is implicated in the "dual recognition" of both peptide and TCR, emphasizing the multiple roles of the class I MHC peptide-binding domain."xsd:string
http://purl.uniprot.org/citations/15131131http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m403372200"xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/author"Beck J.C."xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/author"Baker B.M."xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/author"Biddison W.E."xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/author"Turner R.V."xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/author"Baxter T.K."xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/author"Binz A.K."xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/author"Davis-Harrison R.L."xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/author"Gagnon S.J."xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/pages"29175-29184"xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/title"Strategic mutations in the class I major histocompatibility complex HLA-A2 independently affect both peptide binding and T cell receptor recognition."xsd:string
http://purl.uniprot.org/citations/15131131http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15131131http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15131131
http://purl.uniprot.org/citations/15131131http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15131131
http://purl.uniprot.org/uniprot/#_A0A0A7C548-mappedCitation-15131131http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15131131
http://purl.uniprot.org/uniprot/#_A0A0A7C551-mappedCitation-15131131http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15131131
http://purl.uniprot.org/uniprot/#_A0A0G2R0N3-mappedCitation-15131131http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15131131
http://purl.uniprot.org/uniprot/#_A0A0G2R0N4-mappedCitation-15131131http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15131131
http://purl.uniprot.org/uniprot/#_A0A0G2R0N5-mappedCitation-15131131http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15131131
http://purl.uniprot.org/uniprot/#_A0A076JXB7-mappedCitation-15131131http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15131131
http://purl.uniprot.org/uniprot/#_A0A076L0P9-mappedCitation-15131131http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/15131131