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Abstract：
Tudor domain-containing (TDRD) proteins, as a family of evolutionarily conserved proteins, have been studied extensively in recent years in terms of their biological and biochemical functions. A major function of the TDRD proteins is to recognize the N-terminal arginine-rich motifs of the P-element-induced wimpy testis (PIWI) proteins via their conserved extended Tudor (eTudor or eTud) domains, which is essential in piRNA biogenesis and germ cell development. In this review, we summarize recent progress in the study of the TDRD proteins, and discuss the molecular mechanisms for the different binding selectivity of these eTudor domains to PIWI proteins based on the available binding and structural data. Understanding the binding differences of these TDRDs to PIWI proteins will help us better understand their functional differences and aid us in developing the target-specific therapeutics, because overexpression or mutations of the human TDRD proteins have been demonstrated to associate with various diseases.
摘要：
含有都铎结构域（TDRD）的蛋白质，作为一个进化上保守的蛋白质家族，近年来在其生物和生化功能方面进行了广泛的研究。TDRD蛋白的主要功能是通过其保守的延伸Tudor（eTudor或eTud）结构域识别P元件诱导的弱睾丸（PIWI）蛋白的N端富含精氨酸的基序，这在piRNA生物发生和生殖细胞发育中至关重要。在这次审查中,我们总结了TDRD蛋白研究的最新进展，并根据可用的结合和结构数据讨论这些eTudor结构域对PIWI蛋白的不同结合选择性的分子机制。了解这些TDRDs与PIWI蛋白的结合差异将有助于我们更好地了解它们的功能差异，并帮助我们开发靶向特异性疗法。因为已经证明人类TDRD蛋白的过表达或突变与各种疾病有关。
