NMR backbone assignment of the C\u03b54 domain of immunoglobulin E

Stefi V Benjamin,Alistair J Henry,James M Mcdonnell,Paul I Creeke

doi:10.1007/s12104-020-09936-9

Stefi V Benjamin, Alistair J Henry + Show 2 more

Open Access

https://doi.org/10.1007/s12104-020-09936-9

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Abstract

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.

Highlights

Immunoglobulin E (IgE) is the central effector molecule of allergic reactions (Sutton and Gould 1993)
An allergic reaction is initiated by allergen-mediated crosslinking of FcεRI-bound IgE, leading to activation of effector cells and the subsequent release of inflammatory mediators (Sutton and Gould 1993)
The IgE molecule consists of two identical heavy chains and two identical light chains

Summary

Introduction

Immunoglobulin E (IgE) is the central effector molecule of allergic reactions (Sutton and Gould 1993). Keywords Immunoglobulin E · Cε4 · Homodimer · Backbone assignment · NMR Within IgE-Fc, solution state structural studies of the individual domains provide insights into the allosteric changes that are undergone by the molecule upon ligand binding. We present the backbone NMR assignment for the non-covalent dimer of Cε4.

Results

Conclusion