A range of Câ3-Câ4 interdomain angles in IgE Fc accommodate binding to its receptor CD23.
Acta Crystallogr F Struct Biol Commun
; 70(Pt 3): 305-9, 2014 Mar.
Article
em En
| MEDLINE
| ID: mdl-24598915
ABSTRACT
The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors FcâRI and CD23. FcâRI on mast cells and basophils mediates the immediate hypersensitivity response, whilst the interaction of IgE with CD23 on B cells regulates IgE production. Crystal structures of the lectin-like `head' domain of CD23 alone and bound to a subfragment of IgE consisting of the dimer of Câ3 and Câ4 domains (Fcâ3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23-Fcâ3-4 complex with different molecular-packing constraints is reported, which together with the earlier results demonstrates that conformational variability at the interface extends additionally to the IgE Fc and the quaternary structure of its domains.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Imunoglobulina E
/
Fragmentos Fc das Imunoglobulinas
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Receptores de IgE
Limite:
Humans
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article