– Sugar binding by legume lectins:
– Legume lectins use a framework for binding specific sugars.
– Consists of a conserved monosaccharide binding site with four residues.
– Variable loop confers monosaccharide specificity.
– Subsites around the binding site harbor additional sugar residues.
– Hydrophobic groups are also present.
– Quaternary structure:
– Legume lectins can adopt a wide range of quaternary structures.
– Variability is due to interaction with multivalent ligands.
– Conserved structure of the subunit allows for this variability.
– Quaternary structures of some legume lectins show remarkable diversity.
– Interaction with ligands influences the quaternary structure.
– References:
– Studies on the monosaccharide binding site of lentil lectin.
– Legume lectins constitute a large family of homologous proteins.
– Structural studies on legume lectins have been conducted.
– Signature of quaternary structure found in legume lectin sequences.
– Role of weak protein-protein interactions in multivalent lectin-carbohydrate binding.
– Additional information:
– Legume lectins are structurally interesting proteins.
– They have conserved monosaccharide binding sites.
– Variable loops contribute to monosaccharide specificity.
– Quaternary structures can vary significantly.
– Interaction with ligands influences the protein structure.
– Significance of legume lectins:
– Legume lectins play a crucial role in sugar binding.
– Their structural diversity allows for versatile functions.
– Understanding their quaternary structures is important.
– Weak protein-protein interactions contribute to their binding abilities.
– Legume lectins are valuable molecules for studying protein-carbohydrate interactions.
The legume lectins (or L-type lectins) are a family of sugar-binding proteins or lectins found in the seeds and, in smaller amounts, in the roots, stems, leaves and bark of plants of the family Fabaceae. The exact function of the legume lectins in vivo is unknown but they are probably involved in the defense of plants against predators. Related proteins in other plant families and in animals have also been found. They have been used for decades as a model system for the study of protein-carbohydrate interactions, because they show a wide variety of binding specificities and are easy to obtain, purify, and characterize the structure of. Well-studied members of this protein family include phytohemagglutinin, soybean agglutinins, and concanavalin A.
