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]
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 enhances endothelial cell proliferation and angiogenesis, potentially aiding tumour vascularisation. This contrasts with its tumour-suppressive effects in hepatoma, highlighting context-dependent roles.[9]
^Cavada, Benildo Sousa; Osterne, Vinicius Jose Silva; Lossio, Claudia Figueiredo; Pinto-Junior, Vanir Reis; Oliveira, Messias Vital; Silva, Mayara Torquato Lima; Leal, Rodrigo Bainy; Nascimento, Kyria Santiago (2019-08-01). "One century of ConA and 40 years of ConBr research: A structural review". International Journal of Biological Macromolecules. 134: 901–911. doi:10.1016/j.ijbiomac.2019.05.100. ISSN1879-0003. PMID31108148.
^Burgess, Agathe; Mornon, Jean-Paul; de Saint-Basile, Geneviève; Callebaut, Isabelle (2009-05-15). "A concanavalin A-like lectin domain in the CHS1/LYST protein, shared by members of the BEACH family". Bioinformatics. 25 (10): 1219–1222. doi:10.1093/bioinformatics/btp151. ISSN1367-4811. PMID19289442.
