β1-6 branched N-glycan

**β1-6 branched N-glycans** are structural modifications found on asparagine-linked (N-linked) carbohydrate chains of glycoproteins, generated by the enzyme N-acetylglucosaminyltransferase V (GnT-V/MGAT5)[1][2][8]. This branching occurs by adding a β1-6 linked N-acetylglucosamine (GlcNAc) residue to the α1-6 mannose on the core of N-glycans, leading to tri- or tetra-antennary structures[1][8]. These branched glycans are highly upregulated in cancer cells, where they regulate biological processes such as cell adhesion, growth signaling, and immune evasion—often by modifying key receptors, integrins, or PD-L1[1][2][5][6][11]. While not therapeutic targets themselves, they represent a critical outcome of MGAT5/GnT-V activity and serve as biomarkers of tumor aggressiveness and immune checkpoint therapy response[5][10]. Small-molecule or genetic targeting of the MGAT5 enzyme is an area of active research for cancer therapeutics. Because β1-6 branched N-glycans modify many distinct glycoproteins, targeting their synthesis may cause broad biological effects. **Note:** - This entry is *not* a classical drug target (e.g., receptor, enzyme) but a glycan modification motif. Its “target” is MGAT5/GnT-V—the enzyme catalyzing its biogenesis, which is a bona fide therapeutic target in oncology[1][6]. - If you seek a structured entry for the corresponding enzyme, use “N-acetylglucosaminyltransferase V (MGAT5)” as the canonical_name.

Other names

β1,6-GlcNAc-branched N-glycanβ1,6-branch N-glycanMGAT5 productGnT-V producttri- and tetra-antennary N-glycan (with β1-6 branch)

For enzyme inhibitors (e.g., MGAT5 inhibitors): Inhibit formation of β1-6 branch, reducing glycan-mediated functions on cell surfaces