Skip Navigation

This Article
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Sutton, B. J
Right arrow Articles by Beavil, A. J
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sutton, B. J
Right arrow Articles by Beavil, A. J
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

British Medical Bulletin 56:1004-1018 (2000)
© 2000 The British Council

research-article

Inhibition of lgE-receptor interactions

Brain J Sutton, Rebecca L Beavil and Andrew J Beavil

The Randall Centre for Molecular Mechanisms of Cell Function, King's College London London, UK

Correspondence to:Dr Brain J Sutton, The Raindall Centre for Molecular Mechanisms of Cell function, King's College London, New Hunt's House, Guy's Hospital Campus, London Bridge, London Se1 1UL UK

Abstract

Immunoglobulin E plays a central role in allergic disease and, as our undrestanding of the network of interactions between lgE and its receptors impproves, new opportunities for therapeutic intervention emerge. lgE binding to its ‘high-affinity’ receptor, FCRI, first identified on mast cells and now known to be expressed on a variety of other cell types, is the best characterised interaction, and has attracted most attention. The ‘low affinity’ receptor, FC{varepsilon}RII/CD23, first found on B-cells, appears to be part of a more complex network that has yet to be fully elucidated. Two recent advances concerning the IgE-FCRI interaction are noteworthy. The first is the development of a monoiclonal anti-lgE antibody, now in advanced clinical trials, which minhibits this interaction and certainly proves the viability of this approach. The second is the publication of the crystal structure of the complex between lgE and FC{varepsilon}RI, which opens the way for the first structure-based design of small molecule inhibitors.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.