PMID- 16563391 OWN - NLM STAT- MEDLINE DCOM- 20060504 LR - 20220129 IS - 0014-5793 (Print) IS - 0014-5793 (Linking) VI - 580 IP - 8 DP - 2006 Apr 3 TI - Catalytic folding of the Cepsilon3 domain by its high affinity receptor. PG - 2129-34 AB - 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. FAU - Harwood, Naomi E AU - Harwood NE AD - Laboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. FAU - Price, Nicholas C AU - Price NC FAU - McDonnell, James M AU - McDonnell JM LA - eng GR - G0001352/MRC_/Medical Research Council/United Kingdom GR - G0200486/MRC_/Medical Research Council/United Kingdom GR - WT_/Wellcome Trust/United Kingdom PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20060315 PL - England TA - FEBS Lett JT - FEBS letters JID - 0155157 RN - 0 (Anilino Naphthalenesulfonates) RN - 0 (Immunoglobulin Fc Fragments) RN - 0 (Immunoglobulin epsilon-Chains) RN - 0 (Receptors, IgE) RN - 0 (Recombinant Proteins) RN - 1137-00-4 (7-azatryptophan) RN - 630I4V6051 (1-anilino-8-naphthalenesulfonate) RN - 8DUH1N11BX (Tryptophan) SB - IM MH - Anilino Naphthalenesulfonates/chemistry MH - Animals MH - Catalysis MH - Fluorescence MH - Humans MH - Immunoglobulin Fc Fragments/metabolism MH - Immunoglobulin epsilon-Chains/*chemistry/*metabolism MH - Mice MH - Nuclear Magnetic Resonance, Biomolecular MH - *Protein Folding MH - Protein Structure, Tertiary MH - Receptors, IgE/*metabolism MH - Recombinant Proteins/chemistry/metabolism MH - Spectrometry, Fluorescence MH - Time Factors MH - Tryptophan/analogs & derivatives/chemistry EDAT- 2006/03/28 09:00 MHDA- 2006/05/05 09:00 CRDT- 2006/03/28 09:00 PHST- 2005/09/15 00:00 [received] PHST- 2006/03/01 00:00 [revised] PHST- 2006/03/01 00:00 [accepted] PHST- 2006/03/28 09:00 [pubmed] PHST- 2006/05/05 09:00 [medline] PHST- 2006/03/28 09:00 [entrez] AID - S0014-5793(06)00322-X [pii] AID - 10.1016/j.febslet.2006.03.021 [doi] PST - ppublish SO - FEBS Lett. 2006 Apr 3;580(8):2129-34. doi: 10.1016/j.febslet.2006.03.021. Epub 2006 Mar 15.