{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hoek M"],"funding":["Dutch Research Council (NWO)"],"pagination":["4518-4528"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8419865"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["20(9)"],"pubmed_abstract":["Presentation of antigens by human leukocyte antigen (HLA) complexes at the cell surface is a key process in the immune response. The α-chain, containing the peptide-binding groove, is one of the most polymorphic proteins in the proteome. All HLA class I α-chains carry a conserved N-glycosylation site, but little is known about its nature and function. Here, we report an in-depth characterization of N-glycosylation features of HLA class I molecules. We observe that different HLA-A α-chains carry similar glycosylation, distinctly different from the HLA-B, HLA-C, and HLA-F α-chains. Although HLA-A displays the broadest variety of glycan characteristics, HLA-B α-chains carry mostly mature glycans, and HLA-C and HLA-F α-chains carry predominantly high-mannose glycans. We expected these glycosyl"],"journal":["Journal of proteome research"],"pubmed_title":["Allotype-Specific Glycosylation and Cellular Localization of Human Leukocyte Antigen Class I Proteins."],"pmcid":["PMC8419865"],"funding_grant_id":["ICI00003","184.034.019"],"pubmed_authors":["Hoek M","Heck AJR","Wu W","Demmers LC"],"additional_accession":[]},"is_claimable":false,"name":"Allotype-Specific Glycosylation and Cellular Localization of Human Leukocyte Antigen Class I Proteins.","description":"Presentation of antigens by human leukocyte antigen (HLA) complexes at the cell surface is a key process in the immune response. The α-chain, containing the peptide-binding groove, is one of the most polymorphic proteins in the proteome. All HLA class I α-chains carry a conserved N-glycosylation site, but little is known about its nature and function. Here, we report an in-depth characterization of N-glycosylation features of HLA class I molecules. We observe that different HLA-A α-chains carry similar glycosylation, distinctly different from the HLA-B, HLA-C, and HLA-F α-chains. Although HLA-A displays the broadest variety of glycan characteristics, HLA-B α-chains carry mostly mature glycans, and HLA-C and HLA-F α-chains carry predominantly high-mannose glycans. We expected these glycosyl","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Sep","modification":"2026-05-08T19:16:32.57Z","creation":"2022-02-11T10:21:14.56Z"},"accession":"S-EPMC8419865","cross_references":{"pubmed":["34415762"],"doi":["10.1021/acs.jproteome.1c00466"]}}