Immunoglobulin E (IgE) plays a central role in allergic reactions. IgE is a dynamic molecule that is capable of undergoing large conformational changes. X-ray crystal structures of the Fc region of IgE in complex with various ligands have shown that IgE-Fc can exist in extended and various bent conformations. IgE-Fc consists of three domains: Cε2, Cε3 and Cε4. While the complete NMR backbone assignments of the Cε2 and Cε3 domains have been reported previously, the Cε4 domain has not been assigned. Here, we report the complete backbone assignment of the Cε4 homodimer. Cε4 can be used as a model system to study dynamics and allostery in IgE, as both molecules exist as homodimers and exhibit similar binding properties to a number of ligands.

中文翻译：

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免疫球蛋白 E 的 Cε4 结构域的 NMR 主链分配。

免疫球蛋白 E (IgE) 在过敏反应中发挥着核心作用。IgE 是一种动态分子，能够发生较大的构象变化。IgE Fc区与各种配体复合物的X射线晶体结构表明IgE-Fc可以以延伸和各种弯曲构象存在。IgE-Fc 由三个结构域组成：Cε2、Cε3 和 Cε4。虽然之前已经报道了 Cε2 和 Cε3 结构域的完整 NMR 主链分配，但 Cε4 结构域尚未分配。在这里，我们报告了 Cε4 同二聚体的完整主链分配。Cε4 可用作研究 IgE 动力学和变构的模型系统，因为这两种分子均以同二聚体形式存在，并且与许多配体表现出相似的结合特性。