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).
复制标题
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
中科院分区:
文献类型:
--
作者:
Wang Hongyang;Wang Zhizhi;Tang Qun;Yan Xiao-Xue;Xu Wenqing
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.