Chapter title |
Solution NMR Analysis of O-Glycopeptide-Antibody Interaction.
|
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Chapter number | 26 |
Book title |
Mucins
|
Published in |
Methods in molecular biology, January 2024
|
DOI | 10.1007/978-1-0716-3670-1_26 |
Pubmed ID | |
Book ISBNs |
978-1-07-163669-5, 978-1-07-163670-1
|
Authors |
Kokubu, Ryoka, Ohno, Shiho, Manabe, Noriyoshi, Yamaguchi, Yoshiki |
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. |
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