In this issue of Structure, Viennet et al.¹ report a study characterizing the DNA binding by a three-zinc-finger fragment from the transcription factor BCL11A, with the unusual feature that an interfinger interaction in the free protein is disrupted during binding, which provides a positive entropic contribution that enhances the affinity.

中文翻译：

---

妨碍的手指：当绑定不仅仅是关于绑定状态时


在本期 Structure中，Viennet 等人1 报告了一项研究，该研究表征了来自转录因子 BCL11A 的三锌指片段的 DNA 结合，其不寻常的特征是游离蛋白中的指间相互作用在结合过程中被破坏，这提供了增强的亲和力的正熵贡献。