Structure and Properties
Like most lectins, ConA is a homotetramer: each sub-unit (26.5KDa, 235 amino-acids, heavily glycated) binds a metallic atom (usually Mn2+ and a Ca2+). Its tertiary structure has been elucidated, and the molecular basis of its interactions with metals as well as its affinity for the sugars mannose and glucose are well known.
ConA binds specifically α-D-mannosyl and α-D-glucosyl residues (two hexoses differing only by the alcohol on carbon 2) in terminal position of ramified structures from B-Glycans (reach in α-mannose, or hybrid and bi-antennary glycanes complexes). It has 4 binding sites, corresponding to the 4 sub-units. The molecular weight is 104-112KDa and the isoelectric point (pI) is in the range of 4.5-5.5.
Concanavalin A has a low-frequency wave number of 20 cm−1 in its Raman spectra. This emission has been assigned to the breathing motion of the beta barrel consisting of 14 beta-strands in the concanavalin A molecule.
ConA can also initiate cell division (mitogenesis) principally acting on T-lymphocytes, by stimulating the energy metabolism of thymocytes within seconds of exposure.
For biotechnological uses, see Fluorescent glucose biosensors.Read more about this topic: Concanavalin A
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