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http://purl.uniprot.org/citations/23871486http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23871486http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23871486http://www.w3.org/2000/01/rdf-schema#comment"Nectin and nectin-like proteins are cell adhesion molecules that mediate the formation of cell adherens junctions by forming homo- or heterodimers. Some members of this protein family can also be used by immune receptors to mediate immune recognition. For instance, nectin-like 2 (Necl-2) is used as a ligand for the immune system by interaction with the immune receptor CRTAM (class-I MHC-restricted T cell associated molecule), which is mainly expressed on the surface of cytotoxic lymphocyte cells. However, the Necl-2/CRTAM binding mode and its relationship to cell adhesion are not known. Here, we report a Necl-2/CRTAM complex structure, demonstrating that Necl-2 binding to CRTAM competes with the dimerization of CRTAM and possibly Necl-2. Necl-2 occupies the CRTAM homodimer interface, making homodimerization impossible. Mutational and functional analyses identified key amino acids (double "lock-and-key") responsible for the binding. Our work illustrates how the cell adhesion molecule Necl-2 competitively binds the immune receptor CRTAM."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2013.06.006"xsd:string
http://purl.uniprot.org/citations/23871486http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2013.06.006"xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Gao G.F."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Gao G.F."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Lu G."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Lu G."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Fan Z."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Fan Z."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Qi J."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Qi J."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Zhang Z."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Zhang B."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Zhang B."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Yan J."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/author"Yan J."xsd:string
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23871486http://purl.uniprot.org/core/date"2013"xsd:gYear