Log in to save to my catalogue

Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interact...

Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interact...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_100e1c2461b14a39be4cdf8caf230db8

Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction

About this item

Full title

Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction

Publisher

London: Nature Publishing Group UK

Journal title

Nature communications, 2018-01, Vol.9 (1), p.7-7, Article 7

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Anti-IgE therapeutics interfere with the ability of IgE to bind to its receptors on effector cells. Here we report the crystal structure of an anti-IgE single-domain antibody in complex with an IgE Fc fragment, revealing how the antibody inhibits interactions between IgE and the two receptors FcεRI and CD23. The epitope overlaps only slightly with...

Alternative Titles

Full title

Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_100e1c2461b14a39be4cdf8caf230db8

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_100e1c2461b14a39be4cdf8caf230db8

Other Identifiers

ISSN

2041-1723

E-ISSN

2041-1723

DOI

10.1038/s41467-017-02312-7

How to access this item