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Concanavalin A
3CNA Concanavalin A.png
Crystallographic structure of a tetramer of jack bean concanavalin A (the monomers are colored cyan, green, red, and magenta respectively). Calcium (gold) and maganese cations (grey) are depicted as spheres.[1]
Symbol  ?
UniProt P81461
Other data

Concanavalin A is a lectin protein originally extracted from the jack-bean Canavalia ensiformis. It binds specifically to certain structures found in various sugars, glycoproteins, and glycolipids, mainly internal and nonreducing terminal alpha-mannosyl groups. It was the first lectin to be available on a commercial basis and is widely used in biology and biochemistry to characterize glycoproteins and other sugar-containing entities. It is also used to purify macromolecules in lectin affinity chromatography.[citation needed]

Concanavalin A is also a lymphocyte mitogen. It is also widely believed to be involved in the interaction between alpha-mannosyl oligosaccharides on the surface of the HIV virus and the human T cell lymphocyte, used by the HIV virus to enter the T cell.[citation needed]

It has also been shown as a stimulator of several matrix metalloproteinases (MMPs).[2]

See also


  1. ^ PDB 3CNA; Hardman KD, Ainsworth CF (December 1972). "Structure of concanavalin A at 2.4-A resolution". Biochemistry 11 (26): 4910–9. doi:10.1021/bi00776a006. PMID 4638345. 
  2. ^ Yu M, Sato H, Seiki M, Thompson EW (August 1995). "Complex regulation of membrane-type matrix metalloproteinase expression and matrix metalloproteinase-2 activation by concanavalin A in MDA-MB-231 human breast cancer cells". Cancer Res. 55 (15): 3272–7. PMID 7614461. 

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