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Catalytic folding of the Cepsilon3 domain by its high affinity receptor |
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| Authors: | Harwood Naomi E Price Nicholas C McDonnell James M |
| Institution: | Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. |
| Abstract: | The interaction of immunoglobulin E (IgE) with its cellular receptor FcepsilonRIalpha is a central regulator of allergy. Structural studies have identified the third domain (Cepsilon3) of the constant region of epsilon heavy chain as the receptor binding region. The isolated Cepsilon3 domain is a "molten globule" that becomes structured upon binding of the FcepsilonRIalpha ligand. In this study, fluorescence and nuclear magnetic resonance spectroscopies are used to characterise the role of soluble FcepsilonRIalpha in the folding of the monomeric Cepsilon3 domain of IgE. Soluble FcepsilonRIalpha is shown to display characteristic properties of a catalyst for the folding of Cepsilon3, with the rate of Cepsilon3 folding being dependent on the concentration of the receptor. |
| Keywords: | 7-AW 7-azatryptophan ANS 8-anilinonaphthalene-1-sulfonate Cε3 the third constant domain of IgE FcεRI high affinity receptor for IgE HSQC 1H-15N-heteronuclear single quantum coherence IgE immunoglobulin E IgG immunoglobulin G IPTG d-thiogalactoside" target="_blank">isopropyl β-d-thiogalactoside NMR nuclear magnetic resonance PBS phosphate-buffered saline sFcεRIα the extracellular domains of the α-chain of FcεRI Tm melting temperature |
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