http://purl.uniprot.org/citations/10438516 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10438516 | http://www.w3.org/2000/01/rdf-schema#comment | "Interleukin-16 (IL-16) activates CD4(+) cells, possibly by direct interaction with CD4. IL-16 structure and function are highly conserved across species, suggesting similar conservation of a putative IL-16 binding site on CD4. Comparison of the human CD4 amino acid sequence with that of several different species revealed that immunoglobulin-like domain 4 is the most conserved extracellular region. Potential interaction of this domain with IL-16 was studied by testing murine D4 sequence-based oligopeptides for inhibition of IL-16 chemoattractant activity and inhibition of IL-16 binding to CD4 in vitro. Three contiguous 12-residue D4 region peptides (designated A, B, and C) blocked IL-16 chemoattractant activity, with peptide B the most potent. Peptides A and B were synergistic for inhibition, but peptide C was not. Peptides A and B also blocked IL-16 binding to CD4 in vitro, whereas peptide C did not. CD4, in addition to its known function as a receptor for major histocompatibility complex class II, contains a binding site for IL-16 in the D4 domain. The D4 residues required for IL-16 binding overlap those previously shown to participate in CD4-CD4 dimerization following class II major histocompatibility complex binding, providing a mechanistic explanation for the known function of IL-16 to inhibit the mixed lymphocyte reaction."xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.33.23387"xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/author | "Liu Y."xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/author | "Kornfeld H."xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/author | "Center D.M."xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/author | "Cruikshank W.W."xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/author | "O'Loughlin T."xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/author | "O'Reilly P."xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/pages | "23387-23395"xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/title | "Identification of a CD4 domain required for interleukin-16 binding and lymphocyte activation."xsd:string |
http://purl.uniprot.org/citations/10438516 | http://purl.uniprot.org/core/volume | "274"xsd:string |
http://purl.uniprot.org/citations/10438516 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10438516 |
http://purl.uniprot.org/citations/10438516 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10438516 |
http://purl.uniprot.org/uniprot/#_P01730-mappedCitation-10438516 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10438516 |
http://purl.uniprot.org/uniprot/#_Q14005-mappedCitation-10438516 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/10438516 |
http://purl.uniprot.org/uniprot/P01730 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10438516 |
http://purl.uniprot.org/uniprot/Q14005 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/10438516 |