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Structure and dynamics of IgE–receptor interactions: Fcε RI and CD 23/Fcε RII
Author(s) -
Sutton Brian J.,
Davies Anna M.
Publication year - 2015
Publication title -
immunological reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.839
H-Index - 223
eISSN - 1600-065X
pISSN - 0105-2896
DOI - 10.1111/imr.12340
Subject(s) - immunoglobulin e , receptor , allosteric regulation , immunology , antibody , fragment crystallizable region , biology , microbiology and biotechnology , chemistry , biochemistry
Summary Immunoglobulin E (IgE) is well known for its role in allergic disease, the manifestations of which are mediated through its two Fc receptors, Fcε RI and CD 23 (Fcε RII ). IgE and its interactions with these receptors are therefore potential targets for therapeutic intervention, and exciting progress has been made in this direction. Furthermore, recent structural studies of IgE‐Fc, the two receptors, and of their complexes, have revealed a remarkable degree of plasticity at the IgE– CD 23 interface and an even more remarkable degree of dynamic flexibility within the IgE molecule. Indeed, there is allosteric communication between the two receptor‐binding sites, which we now know are located at some distance from each other in IgE‐Fc (at opposite ends of the Cε3 domain). The conformational changes associated with Fcε RI and CD 23 binding to IgE‐Fc ensure that their interactions are mutually incompatible, and it may be that this functional imperative has driven IgE to evolve such a dynamic structure. Appreciation of these new structural data has revised our view of IgE structure, shed light on the co‐evolution of antibodies and their receptors, and may open up new therapeutic opportunities.