|PROSITE documentation PDOC00278|
Leguminous plants synthesize sugar-binding proteins which are called legume lectins [1,2]. These lectins are generally found in the seeds. The exact function of legume lectins is not known but they may be involved in the attachment of nitrogen-fixing bacteria to legumes and in the protection against pathogens. Legume lectins bind calcium and manganese (or other transition metals).
Legume lectins are synthesized as precursor proteins of about 230 to 260 amino acid residues. Some legume lectins are proteolytically processed to produce two chains: β (which corresponds to the N-terminal) and α (C-terminal). The lectin concanavalin A (conA) from jack bean is exceptional in that the two chains are transposed and ligated (by formation of a new peptide bond). The N-terminus of mature conA thus corresponds to that of the α chain and the C-terminus to the β chain.
We have developed two signature patterns specific to legume lectins: the first is located in the C-terminal section of the β chain and contains a conserved aspartic acid residue important for the binding of calcium and manganese; the second one is located in the N-terminal of the α chain.Last update:
December 2004 / Pattern and text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Sharon N. Lis H.|
|Title||Legume lectins--a large family of homologous proteins.|
|Source||FASEB J. 4:3198-3208(1990).|
|2||Authors||Lis H. Sharon N.|
|Source||Annu. Rev. Biochem. 55:33-37(1986).|