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1H, 13C, and 15N resonance assignments of the N-terminal domain of human TIG3

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Abstract

Human TIG3 protein is a member of H-REV107 protein family which belongs to the type II tumor suppressor family. TIG3 can induce apoptosis in cancer cells, and it also possesses Ca2+-independent phospholipase A1/2 activity. The NMR assignments of the N-terminal domain of TIG3 are essential for its solution structure determination.

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Acknowledgments

All NMR experiments were carried out at Beijing NMR center. This research was supported by Grant 2009CB521703 (to BX) from the 973 Program of China, Grants 31070648 (to BX) and 30800172 (to JL) from the National Science Foundation of China.

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Authors and Affiliations

  1. Beijing Nuclear Magnetic Resonance Center, Peking University, Beijing, 100871, People’s Republic of China

    Lei Wang, Wenyu Yu, Xiaobai Ren, Jian Lin, Changwen Jin & Bin Xia

  2. College of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, People’s Republic of China

    Lei Wang, Xiaobai Ren, Jian Lin, Changwen Jin & Bin Xia

  3. College of Life Science, Peking University, Beijing, 100871, People’s Republic of China

    Wenyu Yu, Changwen Jin & Bin Xia

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  1. Lei Wang
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  2. Wenyu Yu
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  3. Xiaobai Ren
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  4. Jian Lin
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  5. Changwen Jin
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  6. Bin Xia
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Correspondence to Bin Xia.

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Wang, L., Yu, W., Ren, X. et al. 1H, 13C, and 15N resonance assignments of the N-terminal domain of human TIG3. Biomol NMR Assign 6, 201–203 (2012). https://doi.org/10.1007/s12104-012-9357-2

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  • DOI: https://doi.org/10.1007/s12104-012-9357-2

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