PROSITE documentation PDOC00278

Legume lectins signatures




Description

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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

LECTIN_LEGUME_ALPHA, PS00308; Legume lectins alpha-chain signature  (PATTERN)

LECTIN_LEGUME_BETA, PS00307; Legume lectins beta-chain signature  (PATTERN)


References

1AuthorsSharon N., Lis H.
TitleLegume lectins--a large family of homologous proteins.
SourceFASEB J. 4:3198-3208(1990).
PubMed ID2227211

2AuthorsLis H., Sharon N.
SourceAnnu. Rev. Biochem. 55:33-37(1986).



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