BACKGROUND The THAP (Thanatos Associated Proteins) protein family in humans is implicated in various important cellular processes like epigenetic regulation, maintenance of pluripotency, transposition and disorders like cancers and hemophilia. The human THAP protein family which consists of twelve members of different lengths has a well characterized amino terminal, zinc-coordinating, DNA-binding domain called the THAP domain. However, the carboxy terminus of most THAP proteins is yet to be structurally characterized. A coiled coil region is known to help in protein oligomerization in THAP1 and THAP11. It is not known if other human THAP proteins oligomerize. We have used bioinformatic tools to explore the possibility of dimerization of THAP proteins via a coiled coil region. RESULTS Classification of human THAP protein into three size based groups led to the identification of an evolutionarily conserved alpha helical region, downstream of the amino terminal THAP domain. Secondary structure predictions, alpha helical wheel plots and protein models demonstrated the strong possibility of coiled coil formation in this conserved, leucine rich region of all THAP proteins except THAP10. CONCLUSIONS The identification of a predicted oligomerization region in the human THAP protein family opens new directions to investigate the members of this protein family.

中文翻译：

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人类THAP蛋白家族的分类确定了进化上保守的卷曲螺旋区域。

背景技术人类中的THAP（Thanatos相关蛋白）蛋白家族与各种重要的细胞过程有关，如表观遗传调控，多能性维持，转座以及诸如癌症和血友病等疾病。由不同长度的十二个成员组成的人THAP蛋白家族具有特征明确的氨基末端，锌配位的DNA结合结构域，称为THAP结构域。但是，大多数THAP蛋白的羧基末端尚未在结构上进行表征。已知盘绕的盘绕区域有助于THAP1和THAP11中的蛋白质寡聚。尚不清楚其他人类THAP蛋白是否寡聚。我们已经使用生物信息学工具来探索通过盘绕的螺旋区域将THAP蛋白二聚化的可能性。结果将人THAP蛋白分为三个基于大小的组，导致鉴定了氨基末端THAP结构域下游的进化保守α螺旋区。二级结构预测，α螺旋轮图和蛋白质模型证明，在除THAP10外的所有THAP蛋白质的这一保守的，富含亮氨酸的区域中，卷曲螺旋形成的可能性很大。结论在人类THAP蛋白家族中预测的低聚区域的鉴定为研究该蛋白家族的成员提供了新的方向。α螺旋轮图和蛋白质模型证明，在除THAP10外的所有THAP蛋白质的这个保守的，富含亮氨酸的区域中，卷曲螺旋形成的可能性很大。结论在人类THAP蛋白家族中预测的低聚区域的鉴定为研究该蛋白家族的成员提供了新的方向。α螺旋轮图和蛋白质模型证明，在除THAP10外的所有THAP蛋白质的这个保守的，富含亮氨酸的区域中，卷曲螺旋形成的可能性很大。结论在人类THAP蛋白家族中预测的低聚区域的鉴定为研究该蛋白家族的成员提供了新的方向。