Legume lectin structure.

TitleLegume lectin structure.
Publication TypeJournal Article
Year of Publication1998
AuthorsLoris, R., T. W. Hamelryck, J. Bouckaert, and L. Wyns
JournalBiochim Biophys Acta
Date Published1998 Mar 3
KeywordsCarbohydrate Sequence, Concanavalin A, Dimerization, Fabaceae, Lectins, Models, Molecular, Molecular Sequence Data, Mutagenesis, Site-Directed, Plant Lectins, Plants, Medicinal, Protein Conformation

The legume lectins are a large family of homologous carbohydrate binding proteins that are found mainly in the seeds of most legume plants. Despite their strong similarity on the level of their amino acid sequences and tertiary structures, their carbohydrate specificities and quaternary structures vary widely. In this review we will focus on the structural features of legume lectins and their complexes with carbohydrates. These will be discussed in the light of recent mutagenesis results when appropriate. Monosaccharide specificity seems to be achieved by the use of a conserved core of residues that hydrogen bond to the sugar, and a variable loop that determines the exact shape of the monosaccharide binding site. The higher affinity for particular oligosaccharides and monosaccharides containing a hydrophobic aglycon results mainly from a few distinct subsites next to the monosaccharide binding site. These subsites consist of a small number of variable residues and are found in both the mannose and galactose specificity groups. The quaternary structures of these proteins form the basis of a higher level of specificity, where the spacing between individual epitopes of multivalent carbohydrates becomes important. This results in homogeneous cross-linked lattices even in mixed precipitation systems, and is of relevance for their effects on the biological activities of cells such as mitogenic responses. Quaternary structure is also thought to play an important role in the high affinity interaction between some legume lectins and adenine and a series of adenine-derived plant hormones. The molecular basis of the variation in quaternary structure in this group of proteins is poorly understood.

Alternate JournalBiochim. Biophys. Acta
PubMed ID9546043