Abstract
Ricin is a dimeric toxin from the castor bean Ricinus communis, which is composed of a sugar-binding subunit (B) that attaches to receptors on the surfaces of target cells1–4 and a subunit (A) with enzymatic activity that attacks and inactivates ribosomes. We report here that comparison of amino-acid sequence data with high-resolution structure analysis of the ricin B subunit shows it to be the product of a series of gene duplications. The modern protein has two sugar-binding domains, each of which is composed of three copies of a more ancient galactose-binding peptide of about 40 residues.
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Rutenber, E., Ready, M. & Robertus, J. Structure and evolution of ricin B chain. Nature 326, 624–626 (1987). https://doi.org/10.1038/326624a0
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DOI: https://doi.org/10.1038/326624a0
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