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首页> 外文期刊>Chemistry: A European journal >Serine versus Threonine Glycosylation with α-O-GalNAc: Unexpected Selectivity in Their Molecular Recognition with Lectins
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Serine versus Threonine Glycosylation with α-O-GalNAc: Unexpected Selectivity in Their Molecular Recognition with Lectins

机译：丝氨酸对苏氨酸糖基化与α-O-GalNAc：凝集素分子识别中的意外选择性。

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摘要

The molecular recognition of several glycopeptides bearing Tn antigen (a-O-GalNAc-Ser or a-O-GalNAc-Thr) in their structure by three lectins with affinity for this determinant has been analysed. The work yields remarkable results in terms of epitope recognition, showing that the underlying amino acid of Tn (serine or threonine) plays a key role in the molecular recognition. In fact, while Soybean agglutinin and Vicia villosa agglutinin lectins prefer Tn-threonine, Helix pomatia agglutinin shows a higher affinity for the glycopeptides carrying Tn-serine. The different conformational behaviour of the two Tn biological entities, the residues of the studied glycopeptides in the close proximity to the Tn antigen and the topology of the binding site of the lectins are at the origin of these differences.
机译：分析了几种结构中带有Tn抗原（a-O-GalNAc-Ser或a-O-GalNAc-Thr）的糖肽的分子识别，该三种肽对该决定簇具有亲和力。这项工作在表位识别方面取得了令人瞩目的成果，表明Tn的潜在氨基酸（丝氨酸或苏氨酸）在分子识别中起着关键作用。实际上，虽然大豆凝集素和野豌豆凝集素凝集素更喜欢Tn-苏氨酸，但是螺旋果胶凝集素对携带Tn-丝氨酸的糖肽显示出更高的亲和力。这两个Tn生物学实体的不同构象行为，所研究糖肽的紧邻Tn抗原的残基以及凝集素结合位点的拓扑结构是这些差异的起源。

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