Structure of the Fc fragment of human IgE bound to its high-affinity receptor FcεRIα View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-07

AUTHORS

Scott C. Garman, Beth A. Wurzburg, Svetlana S. Tarchevskaya, Jean-Pierre Kinet, Theodore S. Jardetzky

ABSTRACT

The initiation of immunoglobulin-E (IgE)-mediated allergic responses requires the binding of IgE antibody to its high-affinity receptor, Fc epsilonRI. Crosslinking of Fc epsilonRI initiates an intracellular signal transduction cascade that triggers the release of mediators of the allergic response. The interaction of the crystallizable fragment (Fc) of IgE (IgE-Fc) with Fc epsilonRI is a key recognition event of this process and involves the extracellular domains of the Fc epsilonRI alpha-chain. To understand the structural basis for this interaction, we have solved the crystal structure of the human IgE-Fc-Fc epsilonRI alpha complex to 3.5-A resolution. The crystal structure reveals that one receptor binds one dimeric IgE-Fc molecule asymmetrically through interactions at two sites, each involving one C epsilon3 domain of the IgE-Fc. The interaction of one receptor with the IgE-Fc blocks the binding of a second receptor, and features of this interaction are conserved in other members of the Fc receptor family. The structure suggests new approaches to inhibiting the binding of IgE to Fc epsilonRI for the treatment of allergy and asthma. More... »

PAGES

259

Journal

TITLE

Nature

ISSUE

6793

VOLUME

406

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/35018500

    DOI

    http://dx.doi.org/10.1038/35018500

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1040384935

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/10917520


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