A fluorescent biosensor reveals conformational changes in human immunoglobulin E Fc: implications for mechanisms of receptor binding, inhibition, and allergen recognition.
A fluorescent biosensor reveals conformational changes in human immunoglobulin E Fc: implications for mechanisms of receptor binding, inhibition, and allergen recognition.
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DOI：
10.1074/jbc.m111.331967
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发表时间：
2012-05-18
期刊：
影响因子：
--
通讯作者：
Beavil AJ
中科院分区：
文献类型：
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作者：
Hunt J;Keeble AH;Dale RE;Corbett MK;Beavil RL;Levitt J;Swann MJ;Suhling K;Ameer-Beg S;Sutton BJ;Beavil AJ
免疫球蛋白 E (IgE) 抗体在过敏性疾病中发挥作用。 IgE 在溶液中具有弯曲构象，在与 FcεRI 受体结合时变得更加弯曲，但在与抗 IgE 奥马珠单抗结合时弯曲程度较小。构象变化对于 FcεRI 介导的 IgE 活性至关重要。弯曲结构为 IgE-FcεRI 复合物对过敏刺激的敏感性提供了分子原理。
Immunoglobulin E (IgE) antibodies play a role in allergic disease. IgE has a bent conformation in solution that becomes more bent upon binding to the FcεRI receptor, but less bent upon binding the anti-IgE omalizumab. Conformational change is critical for FcεRI-mediated IgE activity. The bent structure provides a molecular rationale for the susceptibility of IgE-FcεRI complexes to allergenic stimulation.