Backbone and side chain resonance assignments of the C-terminal domain of human TGIF1

Biomolecular NMR Assignments
Cong CaiYunhuang Yang

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.

References

Nov 1, 1995·Journal of Biomolecular NMR·F DelaglioA Bax
Apr 13, 1999·Cell·D WottonJ Massagué
Sep 12, 2006·Molecular Genetics and Metabolism·Kenia B El-JaickMaximilian Muenke
Dec 13, 2006·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Nathalie FerrandAzeddine Atfi
Mar 3, 2012·PLoS Genetics·Kenichiro TaniguchiDavid Wotton
Jan 23, 2018·Biochemical and Biophysical Research Communications·Jiang ZhuYunhuang Yang
Jul 27, 2018·Biochimica Et Biophysica Acta. Proteins and Proteomics·Shuangli LiYunhuang Yang
Jul 31, 2018·Nucleic Acids Research·Ewelina GucaMaria J Macias

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