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Identification of the minimal functional fragment of IgE with high affinity binding for its receptor FcepsilonRI

Reference	B13498
Principal Investigator / Supervisor	Professor Brian Sutton
Co-Investigators / Co-Supervisors	Professor Hannah Gould
Institution	King's College London
Department	GKT School of Biomedical Sciences
Funding type	Research
Value (£)	209,980
Status	Completed
Type	Research Grant
Start date	01/06/2001
End date	01/06/2004
Duration	36 months

Abstract

The interaction between IgE and its high affinity receptor is a target for blocking the allergic response. The isolated Cepsilon3 domain of IgE contains all necessary contact residues, yet its affinity is 1000-fold lower than native, and surprisingly it is almost entirely unfolded. We aim to discover the minimal structural requirements for a fully active and folded Cepsilon3 domain, investigating glycosylation, the presence of adjacent Cepsilon2 and Cepsilon4 domains, and Cepsilon3 dimerisation. The folding of Cepsilon3-containing fragments will be assessed by CD, fluorescence and NMR, and activity measured by SPR and cell binding assays. These data will further understanding of recombinant domain folding and define an agent from which to develop a blocking agent for allergy.

Summary

unavailable

Committee	Closed Committee - Biomolecular Sciences (BMS)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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