Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 14, Issue 1, Pages 151-155Publisher
SPRINGER
DOI: 10.1007/s12104-020-09936-9
Keywords
Immunoglobulin E; C epsilon 4; Homodimer; Backbone assignment; NMR
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Funding
- BBSRC [BB/P000436/1]
- Centre for Biomolecular Spectroscopy, King's College London
- Wellcome Trust [085944]
- BBSRC [BB/P000436/1] Funding Source: UKRI
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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: C epsilon 2, C epsilon 3 and C epsilon 4. While the complete NMR backbone assignments of the C epsilon 2 and C epsilon 3 domains have been reported previously, the C epsilon 4 domain has not been assigned. Here, we report the complete backbone assignment of the C epsilon 4 homodimer. C epsilon 4 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.
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