1Y2X

Crystal structure of the tetragonal form of the common edible mushroom (Agaricus bisporus) lectin in complex with T-antigen and N-acetylglucosamine

Summary for 1Y2X

• Entry DOI: 10.2210/pdb1y2x/pdb
• Related: 1Y2T 1Y2U 1Y2V 1Y2W
• Descriptor: lectin, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: abl, agaricus bisporus, lectin, mushroom, t-antigen, sugar binding protein
• Biological source: Agaricus bisporus
• Total number of polymer chains: 4
• Total formula weight: 67117.66

Authors

Carrizo, M.E.,Capaldi, S.,Perduca, M.,Irazoqui, F.J.,Nores, G.A.,Monaco, H.L. (deposition date: 2004-11-23, release date: 2004-12-21, Last modification date: 2024-04-03)

Primary citation

Carrizo, M.E.,Capaldi, S.,Perduca, M.,Irazoqui, F.J.,Nores, G.A.,Monaco, H.L.
The Antineoplastic Lectin of the Common Edible Mushroom (Agaricus bisporus) Has Two Binding Sites, Each Specific for a Different Configuration at a Single Epimeric Hydroxyl
J.Biol.Chem., 280:10614-10623, 2005

PubMed Abstract: 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 beta 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, Galbeta1-3GalNAc, mediator of the antiproliferative effects of the protein, binds at a shallow depression on the surface of the molecule. The binding of N-acetylgalactosamine overlaps with that moiety of the T antigen, but surprisingly, N-acetylglucosamine, which differs from N-acetylgalactosamine only in the configuration of epimeric hydroxyl 4, binds at a totally different site on the opposite side of the helix-loop-helix motif. The lectin thus has two distinct binding sites per monomer that recognize the different configuration of a single epimeric hydroxyl. The structure of the protein and its two carbohydrate-binding sites are described in detail in this study.

PubMed: 15596442
DOI: 10.1074/jbc.M411989200

Experimental method

X-RAY DIFFRACTION (2.36 Å)