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A range of C∊3–C∊4 interdomain angles in IgE Fc accommodate binding to its receptor CD23
The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: Fc∊RI and CD23. Fc∊RI on mast cells and basophils mediates the immediate hypersensitivity response, whilst the interaction of IgE with CD23 on B cells regulates IgE production. Crys...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
International Union of Crystallography
2014
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3944690/ https://www.ncbi.nlm.nih.gov/pubmed/24598915 http://dx.doi.org/10.1107/S2053230X14003355 |
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author | Dhaliwal, Balvinder Pang, Marie O. Y. Yuan, Daopeng Beavil, Andrew J. Sutton, Brian J. |
author_facet | Dhaliwal, Balvinder Pang, Marie O. Y. Yuan, Daopeng Beavil, Andrew J. Sutton, Brian J. |
author_sort | Dhaliwal, Balvinder |
collection | PubMed |
description | The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: Fc∊RI and CD23. Fc∊RI 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 C∊3 and C∊4 domains (Fc∊3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23–Fc∊3-4 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. |
format | Online Article Text |
id | pubmed-3944690 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-39446902014-03-12 A range of C∊3–C∊4 interdomain angles in IgE Fc accommodate binding to its receptor CD23 Dhaliwal, Balvinder Pang, Marie O. Y. Yuan, Daopeng Beavil, Andrew J. Sutton, Brian J. Acta Crystallogr F Struct Biol Commun Structural Communications The antibody IgE plays a central role in allergic disease, functioning principally through two cell-surface receptors: Fc∊RI and CD23. Fc∊RI 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 C∊3 and C∊4 domains (Fc∊3-4) have recently been determined, revealing flexibility in the IgE-binding site of CD23. Here, a new crystal form of the CD23–Fc∊3-4 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. International Union of Crystallography 2014-02-20 /pmc/articles/PMC3944690/ /pubmed/24598915 http://dx.doi.org/10.1107/S2053230X14003355 Text en © Dhaliwal et al. 2014 http://creativecommons.org/licenses/by/2.0/uk/ This is an open-access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Structural Communications Dhaliwal, Balvinder Pang, Marie O. Y. Yuan, Daopeng Beavil, Andrew J. Sutton, Brian J. A range of C∊3–C∊4 interdomain angles in IgE Fc accommodate binding to its receptor CD23 |
title | A range of C∊3–C∊4 interdomain angles in IgE Fc accommodate binding to its receptor CD23 |
title_full | A range of C∊3–C∊4 interdomain angles in IgE Fc accommodate binding to its receptor CD23 |
title_fullStr | A range of C∊3–C∊4 interdomain angles in IgE Fc accommodate binding to its receptor CD23 |
title_full_unstemmed | A range of C∊3–C∊4 interdomain angles in IgE Fc accommodate binding to its receptor CD23 |
title_short | A range of C∊3–C∊4 interdomain angles in IgE Fc accommodate binding to its receptor CD23 |
title_sort | range of c∊3–c∊4 interdomain angles in ige fc accommodate binding to its receptor cd23 |
topic | Structural Communications |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3944690/ https://www.ncbi.nlm.nih.gov/pubmed/24598915 http://dx.doi.org/10.1107/S2053230X14003355 |
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