A modular interface of IL-4 allows for scalable affinity without affecting specificity for the IL-4 receptor |
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Authors: | Michael Kraich Markus Klein Edwin Patiño Henning Harrer Joachim Nickel Walter Sebald Thomas D Mueller |
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Institution: | (1) Lehrstuhl fr Physiologische Chemie II, Theodor-Boveri Institut fr Biowissenschaften (Biozentrum), Universitt Wrzburg, D-97074 Am Hubland, Wrzburg, Germany;(2) Rudolf-Virchow Zentrum, DFG Forschungszentrum fr Experimentelle Biomedizin, Versbacher Str. 9, D-97078 Wrzburg, Germany |
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Abstract: | Background Interleukin 4 (IL-4) is a key regulator of the immune system and an important factor in the development of allergic hypersensitivity.
Together with interleukin 13 (IL-13), IL-4 plays an important role in exacerbating allergic and asthmatic symptoms. For signal
transduction, both cytokines can utilise the same receptor, consisting of the IL-4Rα and the IL-13Rα1 chain, offering an explanation
for their overlapping biological functions. Since both cytokine ligands share only moderate similarity on the amino acid sequence
level, molecular recognition of the ligands by both receptor subunits is of great interest. IL-4 and IL-13 are interesting
targets for allergy and asthma therapies. Knowledge of the binding mechanism will be important for the generation of either
IL-4 or IL-13 specific drugs. |
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