A novel lectin was purified from the fruiting bodies of king bolete mushrooms (Boletus edulis, also called porcino, cep or penny bun). The lectin was structurally characterized i.e its amino acid sequence and three-dimensional structure were determined. The new protein is a homodimer and each protomer folds as β-trefoil domain and therefore we propose the name Boletus edulis lectin (BEL) β-trefoil to distinguish it from the other lectin that has been described in these mushrooms. The lectin has potent anti-proliferative effects on human cancer cells, which confers to it an interesting therapeutic potential as an antineoplastic agent. Several crystal forms of the apoprotein and of complexes with different carbohydrates were studied by X-ray diffraction. The structure of the apoprotein was solved at 1.12 Å resolution. The interaction of the lectin with lactose, galactose, N-acetylgalactosamine and T-antigen disaccharide, Galβ1-3GalNAc, was examined in detail. All the three potential binding sites present in the β-trefoil fold are occupied in at least one crystal form and are described in detail in this paper. No important conformational changes are observed in the lectin when comparing its co-crystals with carbohydrates with those of the ligand-free protein.

译文

从牛肝菌王蘑菇 (牛肝菌,也称为牛肝菌,cep或penny bun) 的子实体中纯化了一种新型凝集素。凝集素的结构表征,即确定其氨基酸序列和三维结构。新蛋白是同型二聚体,每个原聚物都折叠为 β-三叶结构域,因此我们提出了牛肝菌 (Boletus edulis) 凝集素 (BEL) β-三叶,以将其与这些蘑菇中描述的其他凝集素区分开。凝集素对人类癌细胞具有有效的抗增殖作用,这赋予它作为抗肿瘤药的有趣治疗潜力。通过x射线衍射研究了载脂蛋白和与不同碳水化合物的复合物的几种晶体形式。载脂蛋白的结构以1.12的分辨率求解。详细检查了凝集素与乳糖,半乳糖,N-乙酰半乳糖胺和T抗原二糖Galβ1-3GalNAc的相互作用。存在于 β-三叶折叠中的所有三个潜在结合位点均以至少一种晶体形式占据,并在本文中进行了详细描述。将凝集素与碳水化合物的共晶体与无配体蛋白的共晶体进行比较时,未观察到凝集素的重要构象变化。

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