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Catalytic folding of the Cε3 domain by its high affinity receptor
Author(s) -
Harwood Naomi E.,
Price Nicholas C.,
McDonnell James M.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.03.021
Subject(s) - folding (dsp implementation) , chemistry , immunoglobulin domain , molten globule , receptor , biophysics , protein folding , immunoglobulin e , monomer , ligand (biochemistry) , biochemistry , antibody , biology , immunology , organic chemistry , electrical engineering , engineering , polymer
The interaction of immunoglobulin E (IgE) with its cellular receptor FcεRIα is a central regulator of allergy. Structural studies have identified the third domain (Cε3) of the constant region of epsilon heavy chain as the receptor binding region. The isolated Cε3 domain is a “molten globule” that becomes structured upon binding of the FcεRIα ligand. In this study, fluorescence and nuclear magnetic resonance spectroscopies are used to characterise the role of soluble FcεRIα in the folding of the monomeric Cε3 domain of IgE. Soluble FcεRIα is shown to display characteristic properties of a catalyst for the folding of Cε3, with the rate of Cε3 folding being dependent on the concentration of the receptor.