The carbohydrate binding properties of plant lectins have been widely studied and exploited. Because many plant lectins can be readily isolated, numerous studies of
Figure 10 Surface plasmon resonance analysis. A surface displaying ligand is examined under conditions of flow. Injection of lectin results in an increase in signal observed in the association phase of the curve. At equilibrium the surface achieves maximal binding. Measurement of the dissociation can yield off-rates. Competing ligands in solution can also be assayed.
these receptors have been conducted. The results serve as a foundation for understanding protein-carbohydrate interactions. Plant lectins can be classified by their source, and these groups include the legume, cereal, Amaryllidaceae and related families, and Moraceae and Euphorbiaceae lectins . The lectins in all these classes assemble into multimeric proteins and can adopt a range of different quaternary structures including di- and tetrameric arrangements. The multimers formed afford multivalent displays presenting saccharide binding sites in a variety of spacings and orientations with documented multiplicities of 2 to as many as 12 binding sites, as in the case of the snowdrop lectin . X-ray crystallographic studies have revealed the spatial relationships in many of these multiple binding site arrangements [1,5,42,71,72]. With the diversity of multivalent binding site displays and the large amount of structural and biophysical data available on them, highly accessible plant lectins serve as excellent receptors for the study of multivalent protein-carbohydrate interactions.
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