Wurzburg Beth A, Jardetzky Theodore S
Department of Structural Biology, Stanford University, Stanford, CA 94305, USA.
J Mol Biol. 2009 Oct 16;393(1):176-90. doi: 10.1016/j.jmb.2009.08.012. Epub 2009 Aug 13.
The structure of immunoglobulin E (IgE)-Fc(3-4) has been solved in three new crystal forms, providing 13 snapshots of the Fc conformation and revealing a diverse range of open-closed motions among subunit chains and dimers. A more detailed analysis of the open-to-closed motion of IgE-Fc(3-4) was possible with so many structures, and the new structures allow a more thorough examination of the flexibility of IgE-Fc and its implications for receptor binding. The existence of a hydrophobic pocket at the elbow region of the Fc appears to be conformation dependent and suggests a means of regulating the IgE-Fc conformation (and potentially receptor binding) with small molecules.
免疫球蛋白E（IgE）-Fc(3-4)的结构已通过三种新的晶体形式得到解析，提供了13个Fc构象的快照，并揭示了亚基链和二聚体之间多种开闭运动。有了这么多结构，就有可能对IgE-Fc(3-4)从开放到闭合的运动进行更详细的分析，这些新结构使我们能够更全面地研究IgE-Fc的灵活性及其对受体结合的影响。Fc肘部区域疏水口袋的存在似乎取决于构象，并提示了一种用小分子调节IgE-Fc构象（以及潜在的受体结合）的方法。
