Crystal structure of the human high-affinity IgE receptor
Crystal structure of the human high-affinity IgE receptor
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DOI：
10.1016/s0092-8674(00)81719-5
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发表时间：
1998-12-23
期刊：
影响因子：
64.5
通讯作者：
Jardetzky, TS
中科院分区：
文献类型：
--
作者：
Garman, SC;Kinet, JP;Jardetzky, TS
过敏反应是由人类高亲和力 IgE 受体激活肥大细胞引起的。 IgE 介导的过敏反应可能会针对多种环境化合物而发生，但反应的启动需要 IgE 与其高亲和力受体结合。我们以 2.4 埃的分辨率解析了人类 IgE 受体抗体结合域的 X 射线晶体结构。该结构揭示了免疫球蛋白结构域的高度弯曲排列，形成与 IgE 相互作用的扩展凸面。赋予 IgE 分子特异性的突出环从受体表面延伸到四个暴露色氨酸的不寻常排列附近。 IgE 受体的晶体结构为开发新的过敏治疗方法奠定了基础。
Allergic responses result from the activation of mast cells by the human high-affinity IgE receptor. IgE-mediated allergic reactions may develop to a variety of environmental compounds, but the initiation of a response requires the binding of IgE to its high-affinity receptor. We have solved the X-ray crystal structure of the antibody-binding domains of the human IgE receptor at 2.4 Angstrom resolution. The structure reveals a highly bent arrangement of immunoglobulin domains that form an extended convex surface of interaction with IgE. A prominent loop that confers specificity for IgE molecules extends from the receptor surface near an unusual arrangement of four exposed tryptophans. The crystal structure of the IgE receptor provides a foundation for the development of new therapeutic approaches to allergy treatment.