TGIF1 is an essential regulator of cell differentiation in various biological processes, and is associated with holoprosencephaly and many cancers. The C-terminal domain of TGIF1 that was originally defined as repressive domain 2 can interact with a variety of proteins, such as transcription factor Smad2 and co-repressor Sin3A, to mediate the regulative roles of TGIF1 in diverse cell signaling pathways. However, the recognition mechanism of TGIF1 C-terminal domain for different interacting proteins remains unknown. Here, we report the nearly complete ¹H, ¹³C, and ¹⁵N backbone and side chain resonance assignments of TGIF1 C-terminal domain (residues 256–375), laying a foundation for further research on the structure–function relationship of TGIF1.

中文翻译：

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人TGIF1 C末端域的骨干和侧链共振分配。

TGIF1是各种生物学过程中细胞分化的重要调节剂，并与全脑性头癌和许多癌症有关。TGIF1的C端结构域最初被定义为阻抑结构域2，可以与多种蛋白质相互作用，例如转录因子Smad2和共阻遏物Sin3A，以介导TGIF1在多种细胞信号通路中的调节作用。然而，TGIF1 C末端域对不同相互作用蛋白的识别机制仍然未知。在这里，我们报告了TGIF1 C末端结构域（残基256-375）几乎完整的¹ H，¹³ C和¹⁵ N骨架和侧链共振分配，为进一步研究TGIF1的结构-功能关系奠定了基础。