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http://purl.uniprot.org/citations/15534202http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15534202http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15534202http://www.w3.org/2000/01/rdf-schema#comment"The alpha/beta T cell receptor complex transmits signals from MHC/peptide antigens through a set of constitutively associated signaling molecules, including CD3-epsilon/gamma and CD3-epsilon/delta. We report the crystal structure at 1.9-A resolution of a complex between a human CD3-epsilon/delta ectodomain heterodimer and a single-chain fragment of the UCHT1 antibody. CD3-epsilon/delta and CD3-epsilon/gamma share a conserved interface between the Ig-fold ectodomains, with parallel packing of the two G strands. CD3-delta has a more electronegative surface and a more compact Ig fold than CD3-gamma; thus, the two CD3 heterodimers have distinctly different molecular surfaces. The UCHT1 antibody binds near an acidic region of CD3-epsilon opposite the dimer interface, occluding this region from direct interaction with the TCR. This immunodominant epitope may be a uniquely accessible surface in the TCR/CD3 complex, because there is overlap between the binding site of the UCHT1 and OKT3 antibodies. Determination of the CD3-epsilon/delta structure completes the set of TCR/CD3 globular ectodomains and contributes information about exposed CD3 surfaces."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0407359101"xsd:string
http://purl.uniprot.org/citations/15534202http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0407359101"xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/author"Harrison S.C."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/author"Harrison S.C."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/author"Wiley D.C."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/author"Wiley D.C."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/author"Arnett K.L."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/author"Arnett K.L."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/pages"16268-16273"xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/pages"16268-16273"xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/title"Crystal structure of a human CD3-epsilon/delta dimer in complex with a UCHT1 single-chain antibody fragment."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/title"Crystal structure of a human CD3-epsilon/delta dimer in complex with a UCHT1 single-chain antibody fragment."xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/volume"101"xsd:string
http://purl.uniprot.org/citations/15534202http://purl.uniprot.org/core/volume"101"xsd:string
http://purl.uniprot.org/citations/15534202http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15534202
http://purl.uniprot.org/citations/15534202http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15534202
http://purl.uniprot.org/citations/15534202http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15534202
http://purl.uniprot.org/citations/15534202http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15534202