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
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]
References
- ↑ Seetharaman J, Kanigsberg A, Slaaby R, Leffler H, Barondes SH, Rini JM (May 1998). "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. PMID 9582341.
- ↑ Cavada BS, Osterne VJ, Lossio CF, Pinto-Junior VR, Oliveira MV, Silva MT, et al. (August 2019). "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. PMID 31108148.
- ↑ "Concanavalin A-like lectin/glucanase domain superfamily". InterPro. IPR013320. Retrieved 2025-03-28.
- ↑ Dwyer JM, Johnson C (November 1981). "The use of concanavalin A to study the immunoregulation of human T cells". Clinical and Experimental Immunology. 46 (2): 237–249. PMC 1536405. PMID 6461456.
- ↑ Burgess A, Mornon JP, de Saint-Basile G, Callebaut I (May 2009). "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. PMID 19289442.
- ↑ Sun Y, Qiao Z, Muchero W, Chen JG (2020-12-10). "Lectin Receptor-Like Kinases: The Sensor and Mediator at the Plant Cell Surface". Frontiers in Plant Science. 11 596301. Bibcode:2020FrPS...1196301S. doi:10.3389/fpls.2020.596301. PMC 7758398. PMID 33362827.
- ↑ Burgess A, Mornon JP, de Saint-Basile G, Callebaut I (May 2009). "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. PMID 19289442.
- ↑ Pratt J, Roy R, Annabi B (September 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. PMID 22692046.
- ↑ Li JZ, Zhou XX, Wu WY, Qiang HF, Xiao GS, Wang Y, et al. (December 2022). "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. PMC 8725916. PMID 34913414.
