Carbohydrate soybean agglutinin

A. Dessen, D. Gupta, S. Sabesan, C. F. Brewer, and J. C. Sacchettini, X-ray crystal structure of the soybean agglutinin crosslinked with a biantennary analog of the blood group I carbohydrate antigen, Biochemistry, 34 (1995) 4933 1-942. 

The most potent inhibitor described thus far is the type A disaccharide GalNAc(al-3)Gal. However, the addition of an a-L-fucosyl group to the Gal, as occurs in the type A trisaccharide, greatly diminished its activity [168]. A hydrophobic site on soybean agglutinin was identified by its interaction with A-dansylgalactosamine [169]. The soybean lectin possesses four carbohydrate binding sites per molecule, one for each subunit [169]. 

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