Abstract
THE biological activities1–4 of the mitogenic lectin concanavalin A (con A) depend on the binding of the protein to receptors on the cell surface, and this binding can be inhibited by specific saccharides related to D-mannose and D-glucose5. Knowledge of the location and nature of the saccharide-binding site of con A would therefore contribute greatly to understanding the molecular basis of its biological activities. Although the complete amino acid sequence6–8 and three-dimensional structure6,9–11 of con A are known, there has been conflicting evidence on the location of the carbohydrate-binding site. Crystallographic studies with saccharides labelled with heavy atoms indicated that it was in a deep cavity in the molecule, more than 20 Å from the Mn2+ and Ca2+ ions6,9,12 (Fig. 1). Subsequent magnetic resonance measurements13–15 as well as crystallographic considerations16 suggested that the site was 10–12 Å from the metals, and led to the hypothesis that the previously studied saccharides labelled with heavy atoms (for example, o-iodo-phenyl-β-D-glucopyranoside (β-IPG)) were bound by their hydrophobic aglycones, rather than by their saccharide moities9,17.
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BECKER, J., REEKE, G., CUNNINGHAM, B. et al. New evidence on the location of the saccharide-binding site of concanavalin A. Nature 259, 406–409 (1976). https://doi.org/10.1038/259406a0
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DOI: https://doi.org/10.1038/259406a0
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