Structural insights into the interactions between human IgE and its high affinity receptor FcεRI

被引：28

作者：

Wurzburg, BA

Jardetzky, TS

机构：

[1] Northwestern Univ, Dept Biochem Mol Biol & Cell Biol, Evanston, IL 60208 USA

[2] Northwestern Univ, Dept Microbiol & Immunol, Evanston, IL 60208 USA

来源：

MOLECULAR IMMUNOLOGY | 2002年 / 38卷 / 14期

基金：

美国国家卫生研究院;

关键词：

IgE; Fc receptor; Fc epsilon RI; antibody; X-ray crystallography; allergy; asthma; mast cell; structure; drug design; Fe; signal;

D O I：

10.1016/S0161-5890(02)00035-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The interaction of IgE antibodies with the high affinity IgE receptor. FcepsilonRI. is a key step in the initiation of anti-parasitic immunity and allergic reactions, Recent structural Studies of the receptor, the IgE-Fe and the IgE-Fe:FcepsilonRI complex hake revealed how these two proteins interact to prime mast cell responses to antigen. The structures have revealed a novel arrangement for the FcepsilonRl ectodomains that is also observed in homologous members of this antibody receptor family. The crystal Structure of the IgE-Fe:FcepsilonRl complex clarified how a 1:1 complex between the antibody and receptor is formed, with the receptor binding each chain of the antibody Fe dimer. The IgE-Fe Structure in the absence of the receptor revealed the potential for large conformational rearrangements within the IgE that may affect receptor binding. These studies provide the basis, for further investigation of the specificity of anti body : receptor binding and for the development of new treatments for allergic hpersensitivities. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：1063 / 1072

页数：10

共 69 条

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