Fc的构象变化阻止了两个Fcγ受体分子与一个IgG的结合

Immunology today Pub Date : 2000-07-01 DOI:10.1016/S0167-5699(00)01666-2

Koichi Kato , Wolf H Fridman , Yoji Arata , Catherine Sautès-Fridman

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引用次数: 29

摘要

最近对溶液中igg - Fc - γ - r相互作用的核磁共振分析已经确定了Fc区上的Fc - γ - r结合位点，并提供了在相互作用过程中Fc发生构象变化的证据。在这里，Koichi Kato和他的同事讨论了这种构象变化如何解释IgG分子在缺乏抗原交联的情况下无法触发对生物体有害的反应。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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A conformational change in the Fc precludes the binding of two Fcγ receptor molecules to one IgG

Recent NMR analyses of IgG–FcγR interactions in solution have identified the FcγR-binding site on the Fc region and provided evidence for a conformational change in the Fc occurring during the interaction. Here, Koichi Kato and colleagues discuss how this conformational change explains the incapacity of IgG molecules to trigger responses deleterious to the organism, in the absence of antigen cross-linking.

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Immunology today

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