Structure and ligand binding selectivity of the common edible mushroom (Agaricus bisporus) lectin, a protein with two binding sites that recognize the different configuration of a single epimeric hydroxyl

CARRIZO ME; IRAZOQUI FJ; CAPALDI S; PERDUCA M; NORES GA; MONACO HL

JOURNAL OF BIOLOGICAL CHEMISTRY

Año: 2005 vol. 280 p. 10614 - 10614

0021-9258

b> The lectin from the common mushroom Agaricus bisporus, the most popular edible species in Western countries, has potent antiproliferative effects on human epithelial cancer cells, without any apparent cytotoxicity. This property confers to it an important therapeutic potential as an antineoplastic agent. The three-dimensional structure of the lectin was determined by x-ray diffraction. The protein is a tetramer with 222 symmetry, and each monomer presents a novel fold with two sheets connected by a helix-loop-helix motif. Selectivity was studied by examining the binding of four monosaccharides and seven disaccharides in two different crystal forms. The T-antigen disaccharide, Gal