Solution structure of the region 51-160 of human KIN17 reveals an atypical winged helix domain
Solution structure of the region 51-160 of human KIN17 reveals an atypical winged helix domain
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DOI：
10.1110/ps.073079107
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发表时间：
2007-12-01
期刊：
影响因子：
8
通讯作者：
Zinn-Justin, Sophie
中科院分区：
文献类型：
--
作者：
Carlier, Ludovic;Couprie, Joel;Zinn-Justin, Sophie
人KIN 17是一种45 kDa的真核DNA和RNA结合蛋白，在核代谢中起重要作用，特别是在对遗传毒性的一般反应中。它的氨基酸序列包含一个锌指基序（残基28-50）内的30 kDa的N-末端区域保守的酵母到人类，和一个15 kDa的C-末端串联的SH 3样亚结构域（残基268-393）只发现于高等真核生物。在这里，我们报告了人KIN 17的区域51-160的溶液结构。我们发现，这个片段折叠成一个三个α-螺旋束包装对一个三链β-片。它属于有翼螺旋（WH）家族。与类似WH结构域的结构比较揭示了KIN 17 WH模块呈现额外的且高度保守的3（10）-螺旋。此外，KIN 17 WH螺旋H3不像经典DNA结合WH结构域那样带正电荷。因此，人KIN 17区域51-160可能通过其以3（10）-螺旋为中心的保守表面参与蛋白质-蛋白质相互作用。
Human KIN17 is a 45-kDa eukaryotic DNA- and RNA-binding protein that plays an important role in nuclear metabolism and in particular in the general response to genotoxics. Its amino acids sequence contains a zinc finger motif (residues 28-50) within a 30-kDa N-terminal region conserved from yeast to human, and a 15-kDa C-terminal tandem of SH3-like subdomains (residues 268-393) only found in higher eukaryotes. Here we report the solution structure of the region 51-160 of human KIN17. We show that this fragment folds into a three-alpha-helix bundle packed against a three-stranded beta-sheet. It belongs to the winged helix (WH) family. Structural comparison with analogous WH domains reveals that KIN17 WH module presents an additional and highly conserved 3(10)-helix. Moreover, KIN17 WH helix H3 is not positively charged as in classical DNA-binding WH domains. Thus, human KIN17 region 51-160 might rather be involved in protein-protein interaction through its conserved surface centered on the 3(10)-helix.