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首页> 外文期刊>Journal of Molecular Biology >The 1.2 angstrom resolution structure of the Con A-dimannose complex
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The 1.2 angstrom resolution structure of the Con A-dimannose complex

机译：Con A-二甘露糖复合物的1.2埃分辨结构

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摘要

The complex between concanavalin A (Con A) and alpha1-2 mannobiose (mannose alpha1-2 mannose) has been refined to 1.2 Angstrom resolution. This is the highest resolution structure reported for any sugar-lectin complex. As the native structure of Con A to 0.94 Angstrom resolution is already in the database, this gives us a unique opportunity to examine sugar-protein binding at high resolution. These data have allowed us to model a number of hydrogen atoms involved in the binding of the sugar to Con A, using the difference density map to place the hydrogen atoms. This map reveals the presence of the protonated form of Asp208 involved in binding. Asp208 is not protonated in the 0.94 Angstrom native structure. Our results clearly show that this residue is protonated and hydrogen bonds to the sugar. The structure accounts for the higher affinity of the alpha1-2 linked sugar when compared to other disaccharides. This structure identifies different interactions to those predicted by previous modelling studies. We believe that the additional data presented here will enable significant improvements to be made to the sugar-protein modelling algorithms.
机译：伴刀豆球蛋白A（Con A）和α1-2甘露二糖（甘露糖α1-2甘露糖）之间的复合物已精制至1.2埃分辨率。这是报道的任何糖-凝集素复合物的最高分辨率结构。由于数据库中已经存在Con A的自然结构，分辨率为0.94埃，这为我们提供了一个独特的机会来以高分辨率检查糖蛋白结合。这些数据使我们能够使用差异密度图放置氢原子来模拟糖与Con A结合中涉及的多个氢原子。该图揭示了结合中涉及的Asp208的质子化形式的存在。 Asp208在0.94埃的天然结构中未质子化。我们的结果清楚地表明，该残基被质子化并与糖形成氢键。与其他二糖相比，该结构说明了α1-2连接的糖具有更高的亲和力。这种结构确定了与以前的建模研究所预测的相互作用不同的相互作用。我们相信，此处提供的其他数据将使糖-蛋白质建模算法得到重大改进。

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