title: The intrinsic flexibility of IgE and its role in binding FcepsilonRI.
abstract: The interaction between IgE and its high affinity cellular receptor (FcepsilonRI) is an essential step in the development of allergic responses. Studies have identified the third constant domain of IgE (Cepsilon3) as the receptor binding region. The Cepsilon3 domain has unusual structural features; it was found to be a 'molten globule' structure in an isolated form, only assuming a well structured form upon binding to FcepsilonRI. The conformational flexibility intrinsic to the receptor binding portion of the molecule may be useful to IgE in allowing the large allosteric changes postulated to be required for FcepsilonRI engagement. If allosteric inhibitors can be developed then the dynamic properties of the Cepsilon3 domain may provide opportunities for therapeutic intervention in allergic disorders.
authors.affiliation: Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
authors.forename: Naomi E
authors.initials: NE
authors.lastname: Harwood
authors.forename: James M
authors.initials: JM
authors.lastname: McDonnell
mesh_terms: D001665:Binding Sites; D006801:Humans; D006967:Hypersensitivity / Q000276:immunology*; D007073:Immunoglobulin E / Q000737:chemistry / Q000276:immunology*; D011487:Protein Conformation; D017455:Receptors, IgE / Q000737:chemistry / Q000276:immunology*
chemical_list: C502447:MS4A2 protein, human; D017455:Receptors, IgE; D007073:Immunoglobulin E