1y2u: Difference between revisions

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[[Image:1y2u.jpg|left|200px]]
{{Seed}}
[[Image:1y2u.png|left|200px]]


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{{STRUCTURE_1y2u|  PDB=1y2u  |  SCENE=  }}  
{{STRUCTURE_1y2u|  PDB=1y2u  |  SCENE=  }}  


'''Crystal structure of the common edible mushroom (Agaricus bisporus) lectin in complex with Lacto-N-biose'''
===Crystal structure of the common edible mushroom (Agaricus bisporus) lectin in complex with Lacto-N-biose===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15596442}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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., Carrizo ME, Capaldi S, Perduca M, Irazoqui FJ, Nores GA, Monaco HL, J Biol Chem. 2005 Mar 18;280(11):10614-23. Epub 2004 Dec 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15596442 15596442]
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., Carrizo ME, Capaldi S, Perduca M, Irazoqui FJ, Nores GA, Monaco HL, J Biol Chem. 2005 Mar 18;280(11):10614-23. Epub 2004 Dec 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15596442 15596442]
Crystallization and preliminary X-ray study of the common edible mushroom (Agaricus bisporus) lectin., Carrizo ME, Irazoqui FJ, Lardone RD, Nores GA, Curtino JA, Capaldi S, Perduca M, Monaco HL, Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):718-20. Epub 2004, Mar 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15039564 15039564]
[[Category: Agaricus bisporus]]
[[Category: Agaricus bisporus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Lectin]]
[[Category: Lectin]]
[[Category: Mushroom]]
[[Category: Mushroom]]
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