Structural insights into the interactions between human IgE and its high affinity receptor FcepsilonRI.
The interaction of IgE antibodies with the high affinity IgE receptor, FcepsilonRI, is a key step in the initiation of anti-parasitic immunity and allergic reactions. Recent structural studies of the receptor, the IgE-Fc and the IgE-Fc:FcepsilonRI complex have revealed how these two proteins interact to prime mast cell responses to antigen. The structures have revealed a novel arrangement for the FcepsilonRI ectodomains that is also observed in homologous members of this antibody receptor family. The crystal structure of the IgE-Fc:FcepsilonRI complex clarified how a 1:1 complex between the antibody and receptor is formed, with the receptor binding each chain of the antibody Fc dimer. The IgE-Fc structure in the absence of the receptor revealed the potential for large conformational rearrangements within the IgE that may affect receptor binding. These studies provide the basis for further investigation of the specificity of antibody:receptor binding and for the development of new treatments for allergic hypersensitivities.
Wurzburg
Beth A
BA
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, IL 60208-3500, USA.
Jardetzky
Theodore S
TS
D000818:Animals; D000915:Antibody Affinity; D006801:Humans; D007073:Immunoglobulin E / Q000737:chemistry* / Q000276:immunology; D007700:Kinetics; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D017455:Receptors, IgE / Q000737:chemistry* / Q000276:immunology
D017455:Receptors, IgE; D007073:Immunoglobulin E