Quantifying Siglec-sialylated ligand interactions: a versatile ¹⁹F-T₂ CPMG filtered competitive NMR displacement assay.

ABSTRACT: Sialic-acid-binding immunoglobulin-like lectins (Siglecs) are integral cell surface proteins crucial for the regulation of immune responses and the maintenance of immune tolerance through interactions with sialic acids. Siglecs recognize sialic acid moieties, usually found at the end of N-glycan and O-glycan chains. However, the different Siglecs prefer diverse presentations of the recognized sialic acid, depending on the type of glycosidic linkage used to link to the contiguous Gal/GalNAc or sialic acid moieties. This fact, together with possible O- or N-substitutions at the recognized glycan epitope significantly influences their roles in various immune-related processes. Understanding the molecular details of Siglec-sialoglycan interactions is essential for u

SUBMITTER: Atxabal U 

PROVIDER: S-EPMC11234860 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature