Abstract
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.
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We thank for grant supports from the National Natural Science Foundation of China (Grant Numbers: 21575155 and 21703283).
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Cai, C., Nie, Y., Yue, X. et al. Backbone and side chain resonance assignments of the C-terminal domain of human TGIF1. Biomol NMR Assign 13, 357–360 (2019). https://doi.org/10.1007/s12104-019-09905-x
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DOI: https://doi.org/10.1007/s12104-019-09905-x