Recognition of Complex Core‐Fucosylated N‐Glycans by a Mini Lectin,Angewandte Chemie International Edition

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Recognition of Complex Core‐Fucosylated N‐Glycans by a Mini Lectin
Angewandte Chemie International Edition ( IF 16.1 ) Pub Date : 2018-07-18 , DOI: 10.1002/anie.201805165
Aurore Cabanettes ₁ , Lukas Perkams ₂ , Carolina Spies ₂ , Carlo Unverzagt ₂ , Annabelle Varrot ₁

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The mini fungal lectin PhoSL was recombinantly produced and characterized. Despite a length of only 40 amino acids, PhoSL exclusively recognizes N‐glycans with α1,6‐linked fucose. Core fucosylation influences the intrinsic properties and bioactivities of mammalian N‐glycoproteins and its level is linked to various cancers. Thus, PhoSL serves as a promising tool for glycoprofiling. Without structural precedence, the crystal structure was solved using the zinc anomalous signal, and revealed an interlaced trimer creating a novel protein fold termed β‐prism III. Three biantennary core‐fucosylated N‐glycan azides of 8 to 12 sugars were cocrystallized with PhoSL. The resulting highly resolved structures gave a detailed view on how the exclusive recognition of α1,6‐fucosylated N‐glycans by such a small protein occurs. This work also provided a protein consensus motif for the observed specificity as well as a glimpse into N‐glycan flexibility upon binding.

中文翻译：

迷你凝集素识别复杂的核心岩藻糖基化的N-聚糖

微型真菌凝集素PhoSL重组生产和表征。尽管只有40个氨基酸，PhoSL只能识别具有α1,6-连接岩藻糖的N-聚糖。核心岩藻糖基化影响哺乳动物N-糖蛋白的固有特性和生物活性，其水平与各种癌症有关。因此，PhoSL可以用作糖谱分析的有前途的工具。没有结构优先权，就使用锌异常信号解析了晶体结构，并揭示了交错的三聚体，形成了一种称为β-PrismIII的新型蛋白质折叠。用PhoSL将3个8到12个糖的双触角岩藻糖基化N-聚糖叠氮化物共结晶。由此产生的高度解析的结构详细说明了如何通过这种小蛋白质对α1,6-岩藻糖基化的N-聚糖进行独家识别。

更新日期：2018-07-18

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