The two domains of human galectin-8 bind sialyl- and fucose-containing oligosaccharides in an independent manner. A 3D view by using NMR,RSC Chemical Biology

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The two domains of human galectin-8 bind sialyl- and fucose-containing oligosaccharides in an independent manner. A 3D view by using NMR
RSC Chemical Biology ( IF 4.2 ) Pub Date : 2021-4-12 , DOI: 10.1039/d1cb00051a
Marcos Gómez-Redondo ₁ , Sandra Delgado ₁ , Reyes Núñez-Franco ₁ , Gonzalo Jiménez-Osés _{1,

2} , Ana Ardá _{1,

2} , Jesús Jiménez-Barbero _{1,

2,

3} , Ana Gimeno ₁

Affiliation

The interaction of human galectin-8 and its two separate N-terminal and C-terminal carbohydrate recognition domains (CRD) to their natural ligands has been analysed using a synergistic combination of experimental NMR and ITC methods, and molecular dynamics simulations. Both domains bind the minimal epitopes N-acetyllactosamine (1) and Galβ1–3GalNAc (2) in a similar manner. However, the N-terminal and C-terminal domains show exquisite and opposing specificity to bind either Neu5Ac- or Fuc-containing ligands, respectively. Moreover, the addition of the high-affinity ligands specific for one of the CRDs does not make any effect on the binding at the alternative one. Thus, the two CRDs behave independently and may simultaneously target different molecular entities to promote clustering through the generation of supramolecular assemblies.

中文翻译：

人半乳糖凝集素 8 的两个结构域以独立的方式结合含唾液酸和岩藻糖的寡糖。使用 NMR 的 3D 视图

人类半乳糖凝集素 8 及其两个独立的 N 端和 C 端碳水化合物识别域 (CRD) 与其天然配体的相互作用已使用实验 NMR 和 ITC 方法以及分子动力学模拟的协同组合进行了分析。两个结构域都结合最小表位N-乙酰乳糖胺 ( 1 ) 和 Galβ1–3GalNAc ( 2)) 以类似的方式。然而，N 端和 C 端域分别显示出与 Neu5Ac 或 Fuc 配体结合的精致和相反的特异性。此外，添加特异于其中一个 CRD 的高亲和力配体不会对替代的结合产生任何影响。因此，这两个 CRD 行为独立，可以同时靶向不同的分子实体，通过超分子组装的产生促进聚类。

更新日期：2021-04-20

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