{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sidney J"],"funding":["NIAID NIH HHS","PHS HHS"],"pagination":["2492-503"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2935290"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["184(5)"],"pubmed_abstract":["Compared with DR and DQ, knowledge of the binding repertoires and specificities of HLA-DP alleles is somewhat limited. However, a growing body of literature has indicated the importance of DP-restricted responses in the context of cancer, allergy, and infectious disease. In the current study, we developed high-throughput binding assays for the five most common HLA-DPB1 alleles in the general worldwide population. Using these assays on a comprehensive panel of single-substitution analogs and large peptide libraries, we derived novel detailed binding motifs for DPB1*0101 and DPB1*0501. We also derived more detailed quantitative motifs for DPB1*0201, DPB1*0401, and DPB1*0402, which were previously characterized on the basis of sets of eluted ligands and/or limited sets of substituted peptides"],"journal":["Journal of immunology (Baltimore, Md. : 1950)"],"pubmed_title":["Five HLA-DP molecules frequently expressed in the worldwide human population share a common HLA supertypic binding specificity."],"pmcid":["PMC2935290"],"funding_grant_id":["N01 AI040023","N01-700048C","N01AI40024","N01AI40023","N01-AI-40024","HHSH266200400006C","HHSN266200400006C"],"pubmed_authors":["Ngo S","Peters B","Sette A","Steen A","Moore C","Sidney J","Chung J"],"additional_accession":[]},"is_claimable":false,"name":"Five HLA-DP molecules frequently expressed in the worldwide human population share a common HLA supertypic binding specificity.","description":"Compared with DR and DQ, knowledge of the binding repertoires and specificities of HLA-DP alleles is somewhat limited. However, a growing body of literature has indicated the importance of DP-restricted responses in the context of cancer, allergy, and infectious disease. In the current study, we developed high-throughput binding assays for the five most common HLA-DPB1 alleles in the general worldwide population. Using these assays on a comprehensive panel of single-substitution analogs and large peptide libraries, we derived novel detailed binding motifs for DPB1*0101 and DPB1*0501. We also derived more detailed quantitative motifs for DPB1*0201, DPB1*0401, and DPB1*0402, which were previously characterized on the basis of sets of eluted ligands and/or limited sets of substituted peptides","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Mar","modification":"2025-04-05T00:25:36.827Z","creation":"2019-03-26T23:42:52Z"},"accession":"S-EPMC2935290","cross_references":{"pubmed":["20139279"],"doi":["10.4049/jimmunol.0903655"]}}