title: Analysis of the conformation and thermal stability of the high-affinity IgE Fc receptor β chain polymorphic proteins.
abstract: The high-affinity IgE Fc receptor (FcεRI) β chain acts as a signal amplifier through the immunoreceptor tyrosine-based activation motif in its C-terminal intracellular region. Polymorphisms in FcεRI β have been linked to atopy, asthma, and allergies. We investigated the secondary structure, conformation, and thermal stability of FcεRI β polymorphic (β-L172I, β-L174V, and β-E228G) proteins. Polymorphisms did not affect the secondary structure and conformation of FcεRI β. However, we calculated Gibbs free energy of unfolding (ΔGunf) and significant differences were observed in ΔGunf values between the wild-type FcεRI β (β-WT) and β-E228G. These results suggested that β-E228G affected the thermal stability of FcεRI β. The role of β-E228G in biological functions and its involvement in allergic reactions have not yet been elucidated in detail; therefore, differences in the thermal stability of β-E228G may affect the function of FcεRI β.
authors.affiliation: a Department of Physiology and Biophysics , Gifu University Graduate School of Medicine , Gifu , Japan.
authors.forename: Tomoyoshi
authors.initials: T
authors.lastname: Terada
authors.affiliation: a Department of Physiology and Biophysics , Gifu University Graduate School of Medicine , Gifu , Japan.
authors.forename: Teppei
authors.initials: T
authors.lastname: Takahashi
authors.affiliation: a Department of Physiology and Biophysics , Gifu University Graduate School of Medicine , Gifu , Japan.|b Department of Early Childhood Education , Chubu-gakuin College , Seki , Japan.
authors.forename: Hajime
authors.initials: H
authors.lastname: Arikawa
authors.affiliation: a Department of Physiology and Biophysics , Gifu University Graduate School of Medicine , Gifu , Japan.
authors.forename: Seiichi
authors.initials: S
authors.lastname: Era
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D011110:Polymorphism, Genetic; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D000072417:Protein Domains; D055550:Protein Stability; D058767:Protein Unfolding; D017455:Receptors, IgE / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D013816:Thermodynamics
chemical_list: C521907:Fc-epsilon receptor I beta-chain, mouse; D017455:Receptors, IgE; D011994:Recombinant Proteins
keywords: Gibbs free energy; high-affinity IgE Fc receptor (FcεRI) β chain; polymorphism; thermal stability