Galectin-9 C-terminal carbohydrate recognition domain (Gal-9C)

The galectin-9 C-terminal carbohydrate recognition domain (CRD) is one of two functional domains of the galectin-9 protein, which is a β-galactoside-binding lectin implicated in diverse biological activities, including immune regulation, apoptosis, inflammation, and cell differentiation. The C-terminal domain (Gal-9C) differs from the N-terminal domain in amino acid sequence and ligand specificity, binding unique carbohydrate structures and playing a crucial role in triggering T cell apoptosis and modulating immune cell signaling. Galectin-9 and its CRDs are widely expressed in immune and non-immune tissues and play important roles in both physiological regulation and in the pathogenesis of diseases such as cancer, autoimmunity, and infection. The galectin-9 C-terminal CRD binds to branched N-glycans, linear poly-N-acetyllactosamines, and sialylated oligosaccharides, and has unique receptor interactions compared to other galectins

Other names

Gal-9ChG9CC-terminal CRD of galectin-9

Carbohydrate ligand binding, leading to modulation of cell signaling or induction of apoptosis (especially T cell death) Immune checkpoint modulation (notably via TIM-3 binding on T cells)