Concanavalin domain

Not to be confused with Concanavalin A, a particular protein with this structural fold.

In molecular biology the superfamily concanavalin is named after Concanavalin A (ConA), a well-studied lectin originally extracted from the jack-bean (Canavalia ensiformis). This superfamily includes a diverse range of carbohydrate binding domains and glycosyl hydrolase enzymes that share a common structure.^[2]

Concanavalin
Cartoon representation of the molecular structure of the crystal structure of the human galectin-3 carbohydrate recognition domain (PDB: 1a3k​)[1]
Identifiers
Symbol	Concanavalin
Pfam clan	CL0004
ECOD	10.1
InterPro	IPR013320

Structure

The superfamily is characterised by a sandwich structure arranged in two sheets with a complex topology.^[3]

Examples

• Concanavalin A (ConA): A homotetramer that binds specifically to certain sugars, glycoproteins, and glycolipids. It has applications in biology and biochemistry for characterising glycoproteins and purifying glycosylated macromolecules.^[4]
• CHS1/LYST Protein: Contains a ConA-like lectin domain, suggesting a role in oligosaccharide binding associated with protein traffic and sorting along the secretory pathway.^[5]
• Lectin Receptor-like Kinases: Some plant proteins, such as LecRK-I.9, combine a ConA-like lectin domain with a protein kinase domain, involved in protein-protein interactions and cell wall-plasma membrane signalling.^[6]

Clinical significance

• The ConA-like domain in CHS1/LYST is critical for lysosome function. Its disruption leads to Chediak-Higashi syndrome, characterised by immune dysfunction and albinism.^[7]
• ConA promotes autophagy in glioblastoma cells.^[8]
• ConA enhances endothelial cell proliferation and angiogenesis, potentially aiding tumour vascularisation. This contrasts with its tumour-suppressive effects in hepatoma, highlighting context-dependent roles.^[9]