{"title":"Solution NMR Analysis of O-Glycopeptide-Antibody Interaction.","authors":"Ryoka Kokubu, Shiho Ohno, Noriyoshi Manabe, Yoshiki Yamaguchi","doi":"10.1007/978-1-0716-3670-1_26","DOIUrl":null,"url":null,"abstract":"<p><p>O-Linked glycans potentially play a functional role in cellular recognition events. Recent structural analyses suggest that O-glycosylation can be a specific signal for a lectin receptor which recognizes both the O-glycan and the adjacent polypeptide region. Further, certain antibodies specifically bind to the O-glycosylated peptide. There is growing interest in the mechanism by which O-glycans on proteins are specifically recognized by lectins and antibodies. The recognition system may be common to many O-glycosylated proteins; however, there is limited 3D structural information on the dual recognition of glycan and protein. This chapter describes a solution NMR analysis of the interaction between MUC1 O-glycopeptide and anti-MUC1 antibody MY.1E12.</p>","PeriodicalId":18490,"journal":{"name":"Methods in molecular biology","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2024-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Methods in molecular biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/978-1-0716-3670-1_26","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 0
Abstract
O-Linked glycans potentially play a functional role in cellular recognition events. Recent structural analyses suggest that O-glycosylation can be a specific signal for a lectin receptor which recognizes both the O-glycan and the adjacent polypeptide region. Further, certain antibodies specifically bind to the O-glycosylated peptide. There is growing interest in the mechanism by which O-glycans on proteins are specifically recognized by lectins and antibodies. The recognition system may be common to many O-glycosylated proteins; however, there is limited 3D structural information on the dual recognition of glycan and protein. This chapter describes a solution NMR analysis of the interaction between MUC1 O-glycopeptide and anti-MUC1 antibody MY.1E12.
O 型连接聚糖可能在细胞识别事件中发挥功能性作用。最近的结构分析表明，O-糖基化可以成为凝集素受体的特异信号，这种受体既能识别 O-糖，也能识别邻近的多肽区。此外，某些抗体会特异性地与 O 型糖基化肽结合。人们对凝集素和抗体特异性识别蛋白质上的 O 型糖的机制越来越感兴趣。这种识别系统可能是许多 O 型糖基化蛋白质所共有的；然而，关于糖基和蛋白质双重识别的三维结构信息却很有限。本章介绍了 MUC1 O 型糖肽与抗 MUC1 抗体 MY.1E12 之间相互作用的溶液核磁共振分析。
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