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Ebf1:DNA 复合物的结构揭示了与 Rel 蛋白不同寻常的 DNA 识别和结构同源性。

Structure of an Ebf1:DNA complex reveals unusual DNA recognition and structural homology with Rel proteins.

机构信息

Department of Cellular and Molecular Immunology, Max Planck Institute of Immunobiology, 79108 Freiburg, Germany.

出版信息

Genes Dev. 2010 Oct 15;24(20):2270-5. doi: 10.1101/gad.1976610. Epub 2010 Sep 28.

Abstract

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.

摘要

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。

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