Solution NMR Analysis of O-Glycopeptide-Antibody Interaction.
Antibody
Epitope mapping
MUC1
NMR
O-Glycopeptide
Signal assignment
Titration
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2024
2024
Historique:
medline:
13
2
2024
pubmed:
13
2
2024
entrez:
12
2
2024
Statut:
ppublish
Résumé
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.
Identifiants
pubmed: 38347421
doi: 10.1007/978-1-0716-3670-1_26
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
321-327Informations de copyright
© 2024. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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