Analysis of the conformation and thermal stability of the high-affinity IgE Fc receptor β chain polymorphic proteins*
| Autor: | Tomoyoshi Terada, Hajime Arikawa, Teppei Takahashi, Seiichi Era |
|---|---|
| Rok vydání: | 2016 |
| Předmět: |
Protein Conformation
alpha-Helical 0301 basic medicine Fc receptor Gene Expression Immunoglobulin E Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry Atopy 03 medical and health sciences 0302 clinical medicine Protein Domains Escherichia coli medicine Thermal stability Amino Acid Sequence Tyrosine Molecular Biology Protein secondary structure Protein Unfolding Polymorphism Genetic biology Protein Stability Receptors IgE Chemistry Circular Dichroism Organic Chemistry General Medicine medicine.disease Recombinant Proteins Signal amplifier 030104 developmental biology biology.protein Thermodynamics Protein Conformation beta-Strand 030217 neurology & neurosurgery Intracellular Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 80:1356-1361 |
| ISSN: | 1347-6947 0916-8451 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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