The crystal structure of an avian IgY-Fc fragment reveals conservation with both mammalian IgG and IgE.
The crystal structure of an avian IgY-Fc fragment reveals conservation with both mammalian IgG and IgE.
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DOI：
10.1021/bi8019993
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发表时间：
2009-01
期刊：
影响因子：
2.9
通讯作者：
A. I. Taylor;S. Fabiane;B. Sutton;R. Calvert
中科院分区：
文献类型：
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作者：
A. I. Taylor;S. Fabiane;B. Sutton;R. Calvert
禽类IgY与哺乳动物免疫球蛋白和免疫球蛋白E的祖先密切相关，从而为抗体结构和功能的进化提供了新的线索。表达和结晶了由CuPsilon3和CuPsilon4结构域的二聚体组成的IgY-Fc重组片段Fcusilon3-4，并测定了其X射线结构，分辨率为1.75A。Fcusilon3-4是迄今为止确定的唯一的非哺乳动物Fc片段结构，并为抗体结构的古老起源提供了第一个结构证据。Fcusilon3-4结构揭示了IgE-Fc和Ig G-Fc的共同特征，并讨论了IgY与其受体结合的意义。
Avian IgY is closely related to an ancestor of both mammalian IgG and IgE and thus provides insights into the evolution of antibody structure and function. A recombinant fragment of IgY-Fc consisting of a dimer of the Cupsilon3 and Cupsilon4 domains, Fcupsilon3-4, was expressed and crystallized and its X-ray structure determined to 1.75 A resolution. Fcupsilon3-4 is the only nonmammalian Fc fragment structure determined to date and provides the first structural evidence for an ancient origin of antibody architecture. The Fcupsilon3-4 structure reveals features common to both IgE-Fc and IgG-Fc, and the implications for IgY binding to its receptor are discussed.