The crystal structure of IgE Fc reveals an asymmetrically bent conformation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2002-07

AUTHORS

Tommy Wan, Rebecca L. Beavil, Stella M. Fabiane, Andrew J. Beavil, Maninder K. Sohi, Maura Keown, Robert J. Young, Alistair J. Henry, Ray J. Owens, Hannah J. Gould, Brian J. Sutton

ABSTRACT

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. More... »

PAGES

681-686

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ni811

DOI

http://dx.doi.org/10.1038/ni811

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046652146

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12068291


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