Concanavalin domain
| 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 |
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
[edit]The superfamily is characterised by a sandwich structure arranged in two sheets with a complex topology.[3]
Examples
[edit]- 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
[edit]- 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]
References
[edit]- ^ Seetharaman, J; Kanigsberg, A; Slaaby, R; Leffler, H; Barondes, S H; Rini, J M (1998-05-01). "X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution". The Journal of Biological Chemistry. 273 (21): 13047–13052. doi:10.1074/jbc.273.21.13047. ISSN 1083-351X. PMID 9582341.
- ^ 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. ISSN 1879-0003. PMID 31108148.
- ^ "InterPro". ebi.ac.uk. Retrieved 2025-03-28.
- ^ Dwyer, J. M.; Johnson, C. (1981). "The use of concanavalin A to study the immunoregulation of human T cells". Clinical and Experimental Immunology. 46 (2): 237–249. ISSN 0009-9104. PMC 1536405. PMID 6461456.
- ^ 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 (Oxford, England). 25 (10): 1219–1222. doi:10.1093/bioinformatics/btp151. ISSN 1367-4811. PMID 19289442.
- ^ Sun, Yali; Qiao, Zhenzhen; Muchero, Wellington; Chen, Jin-Gui (2020-12-10). "Lectin Receptor-Like Kinases: The Sensor and Mediator at the Plant Cell Surface". Frontiers in Plant Science. 11. doi:10.3389/fpls.2020.596301. ISSN 1664-462X. PMC 7758398. PMID 33362827.
- ^ Burgess, Agathe; Mornon, Jean-Paul; de Saint-Basile, Geneviève; Callebaut, Isabelle (2009-05-01). "A concanavalin A-like lectin domain in the CHS1/LYST protein, shared by members of the BEACH family". Bioinformatics (Oxford, England). 25 (10): 1219–1222. doi:10.1093/bioinformatics/btp151. ISSN 1367-4811. PMID 19289442.
- ^ Pratt, Jonathan; Roy, René; Annabi, Borhane (2012). "Concanavalin-A-induced autophagy biomarkers requires membrane type-1 matrix metalloproteinase intracellular signaling in glioblastoma cells". Glycobiology. 22 (9): 1245–1255. doi:10.1093/glycob/cws093. ISSN 1460-2423. PMID 22692046.
- ^ Li, Jing-Zhou (2022-12-31). "Concanavalin A promotes angiogenesis and proliferation in endothelial cells through the Akt/ERK/Cyclin D1 axis". Pharmaceutical Biology. 60 (1): 65–74. doi:10.1080/13880209.2021.2013259. ISSN 1388-0209. PMC 8725916. PMID 34913414.