Identification of a secondary binding site in human macrophage galactose-type lectin by microarray studies: Implications for the molecular recognition of its ligands.

ABSTRACT: The human macrophage galactose-type lectin (MGL) is a C-type lectin characterized by a unique specificity for terminal GalNAc residues present in the tumor-associated Tn antigen (αGalNAc-Ser/Thr) and its sialylated form, the sialyl-Tn antigen. However, human MGL has multiple splice variants, and whether these variants have distinct ligand-binding properties is unknown. Here, using glycan microarrays, we compared the binding properties of the short MGL 6C (MGL^short) and the long MGL 6B (MGL^long) splice variants, as well as of a histidine-to-threonine mutant (MGL^short H259T). Although the MGL^short and MGL^long variants displayed similar binding properties on the glycan array, the MGL^short H259T mutant failed to interact with th

SUBMITTER: Marcelo F 

PROVIDER: S-EPMC6349122 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature