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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent
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Structural insights into Aspergillus fumigatus lectin specificity: AFL binding sites are functionally non-equivalent

机译：结构的见解来自烟曲霉菌凝集素特异性:AFL结合位点在功能上等效

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摘要

The Aspergillus fumigatus lectin AFL was recently described as a new member of the AAL lectin family. As a lectin from an opportunistic pathogen, it might play an important role in the interaction of the pathogen with the human host. A detailed study of structures of AFL complexed with several monosaccharides and oligosaccharides, including blood-group epitopes, was combined with affinity data from SPR and discussed in the context of previous findings. Its six binding sites are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition. AFL displays a high affinity in the micromolar range towards oligosaccharides which were detected in plants and also those bound on the human epithelia. All of these results indicate AFL to be a complex member of the lectin family and a challenging target for future medical research and, owing to its binding properties, a potentially useful tool in specific biotechnological applications.
机译：来自烟曲霉菌的凝集素AFL最近描述为一个AAL凝集素的新成员家庭。病原体,它可能扮演重要的角色人类宿主病原体的相互作用。AFL多元结构的详细研究与多个单糖,寡糖,包括血型抗原表位,结合从SPR和关联数据吗在先前发现的背景下讨论。它的六个结合位点是等效,由于氨基酸的细微差异构成他们表现出明显差异特定的配体识别。亲和力在微摩尔的范围内寡糖在植物中发现以及那些束缚人的上皮细胞。这些结果表明澳式足球联盟是一个复杂的凝集素家族的成员和挑战性未来的医学研究和目标,由于它的绑定属性,一个潜在的有用的工具在特定的生物技术的应用程序。

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