Neuhaus David, Stott Katherine
MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK.
Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, UK.
Structure. 2024 Dec 5;32(12):2182-2185. doi: 10.1016/j.str.2024.11.001.
In this issue of Structure, Viennet et al. 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.
在本期《结构》杂志中,维涅特等人报告了一项研究,该研究对转录因子BCL11A的一个三锌指片段与DNA的结合进行了表征,其不同寻常之处在于,游离蛋白质中的指间相互作用在结合过程中被破坏,这提供了一个正向熵贡献,增强了亲和力。