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The distinguishing structural feature of immunoglobulin E (IgE), the antibody responsible for allergic hypersensitivity, is the C epsilon 2 domain pair that replaces the hinge region of IgG. The crystal structure of the IgE Fc (constant fragment) at a 2.6-A resolution has revealed these domains. They display a distinctive, disulfide-linked Ig domain interface and are folded back asymmetrically onto the C epsilon 3 and C epsilon 4 domains, which causes an acute bend in the IgE molecule. The structure implies that a substantial conformational change involving C epsilon 2 must accompany binding to the mast cell receptor Fc epsilon RI. This may be the basis of the exceptionally slow dissociation rate of the IgE-Fc epsilon RI complex and, thus, of the ability of IgE to cause persistent allergic sensitization of mast cells.

Original publication

DOI

10.1038/ni811

Type

Journal article

Journal

Nat Immunol

Publication Date

07/2002

Volume

3

Pages

681 - 686

Keywords

Carbohydrate Conformation, Crystallography, X-Ray, Dimerization, Humans, Immunoglobulin Constant Regions, Immunoglobulin E, Models, Molecular, Protein Structure, Tertiary, Receptors, IgE