Department of Cellular and Molecular Immunology, Max Planck Institute of Immunobiology, 79108 Freiburg, Germany.
Genes Dev. 2010 Oct 15;24(20):2270-5. doi: 10.1101/gad.1976610. Epub 2010 Sep 28.
Early B-cell factor 1 (Ebf1) is a key transcriptional determinant of B-lymphocyte differentiation whose DNA-binding domain has no sequence similarity to other transcription factor families. Here we report the crystal structure of an Ebf1 dimer bound to its palindromic recognition site. The DNA-binding domain adopts a pseudoimmunoglobulin-like fold with novel topology, but is structurally similar to the Rel homology domains of NFAT and NF-κB. Ebf1 contacts the DNA with two loop-based modules and a unique Zn coordination motif whereby each Ebf1 monomer interacts with both palindromic half-sites. This unusual mode of DNA recognition generates an extended contact area that may be crucial for the function of Ebf1 in chromatin.
早期 B 细胞因子 1（Ebf1）是 B 淋巴细胞分化的关键转录决定因子，其 DNA 结合域与其他转录因子家族没有序列相似性。在这里，我们报告了一个 Ebf1 二聚体与它的回文识别位点结合的晶体结构。DNA 结合域采用一种具有新颖拓扑结构的假免疫球蛋白样折叠，但在结构上与 NFAT 和 NF-κB 的 Rel 同源结构域相似。Ebf1 与两条基于环的模块和一个独特的 Zn 配位基序与 DNA 结合，其中每个 Ebf1 单体与两个回文半位点相互作用。这种不寻常的 DNA 识别模式产生了一个扩展的接触面积，这对于 Ebf1 在染色质中的功能可能是至关重要的。
