Crystal structure of the LUFS domain of human single-stranded DNA binding Protein 2 (SSBP2).

Crystal structure of the LUFS domain of human single-stranded DNA binding Protein 2 (SSBP2).
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人类单链 DNA 结合蛋白 2 (SSBP2) LUFS 结构域的晶体结构。

DOI:
10.1002/pro.3581
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发表时间:
2019
期刊:
影响因子:
8
通讯作者:
Xu Wenqing
Xu Wenqing
中科院分区:
生物学3区
文献类型:
--
作者:
Wang Hongyang;Wang Zhizhi;Tang Qun;Yan Xiao-Xue;Xu Wenqing

文献摘要

相似文献

人类单链DNA结合蛋白2 (SSBP2)是一种涉及多种癌症形式的肿瘤抑制因子。预计SSBP2和相关的SSBP3/SSBP4蛋白除了其高度保守的N端LUFS (LUG/LUH, Flo8和SSBP/SSDP)结构域外,本质上是无序的。LUFS结构域存在于许多蛋白质中,包括一些转录辅助抑制因子。虽然LUFS结构域包含一个N端Lis同源(LisH)基序,通常形成稳定的二聚体,但没有任何LUFS结构域的3D结构可用。在这里,我们报告了人类SSBP2 LUFS结构域的晶体结构,分辨率为1.52 Å。我们发现SSBP2 LUFS结构域形成了一个四聚体,并揭示了LisH基序的α -螺旋C -末端如何介导SSBP2四聚体(二聚体的二聚体)。LUFS结构域之间四聚界面的守恒表明,其他LUFS结构域也可能以类似的方式形成四聚体。
The human single‐stranded DNA binding Protein 2 (SSBP2) is a tumor suppressor implicated in multiple cancer forms. The SSBP2 and related SSBP3/SSBP4 proteins are predicted to be intrinsically disordered excepted for their highly conserved N‐terminal LUFS (LUG/LUH, Flo8, and SSBP/SSDP) domain. LUFS domains are found in a number of proteins including some transcriptional co‐repressors. Although LUFS domains contain an N‐terminal Lis homology (LisH) motif that typically forms a stable dimer, no 3D structure of any LUFS domain is available. Here, we report a crystal structure of the LUFS domain of human SSBP2 at 1.52 Å resolution. We show that the SSBP2 LUFS domain forms a homo‐tetramer and reveal how an alpha‐helix C‐terminal to the LisH motif mediates SSBP2 tetramerization (dimerization of dimers). Conservation of the tetramerization interface among LUFS domains suggests that other LUFS domains may also form tetramers in similar manners.