Benjamin Stefi V, Creeke Paul I, Henry Alistair J, McDonnell James M
Randall Centre for Cell & Molecular Biophysics, King's College London, New Hunt's House, Guy's Campus, London, SE1 1UL, UK.
UCB Pharma, 216 Bath Road, Slough, Berkshire, SL1 3WE, UK.
Biomol NMR Assign. 2020 Apr;14(1):151-155. doi: 10.1007/s12104-020-09936-9. Epub 2020 Feb 27.
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.
免疫球蛋白E（IgE）在过敏反应中起核心作用。IgE是一种动态分子，能够发生大的构象变化。IgE与各种配体复合物的Fc区域的X射线晶体结构表明，IgE-Fc可以以伸展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主链归属，但Cε4结构域尚未归属。在此，我们报道了Cε4同二聚体的完整主链归属。Cε4可作为研究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，并且对多种配体表现出相似的结合特性。
