Abstract
KIN is a DNA/RNA-binding protein conserved evolutionarily from yeast to humans and expressed ubiquitously in mammals. It is an essential nuclear protein involved in numerous cellular processes, such as DNA replication, class-switch recombination, cell cycle regulation, and response to UV or ionizing radiation-induced DNA damage. The C-terminal region of the human KIN (hKIN) protein is composed of an SH3-like tandem domain, which is crucial for the anti-proliferation effect of the full-length protein. Herein, we present the 1H, 15N, and 13C resonances assignment of the backbone and side chains for the SH3-like tandem domain of the hKIN protein, as well as the secondary structure prediction based on the assigned chemical shifts using TALOS-N software. This work prepares the ground for future studies of RNA-binding and backbone dynamics.
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Acknowledgements
The author IOL thanks the scholarship of CNPq (141886/2019-6). The author IPC gratefully acknowledges the postdoctoral fellowship and financial support from FAPERJ (202.279/2018) and the PROPe UNESP. FAVS thanks to Fundação Araucaria (40/2016) for financial support.
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de Lourenço, I.O., Seixas, F.A.V., Fernandez, M.A. et al. 1H, 15N, and 13C resonance assignments of the SH3-like tandem domain of human KIN protein. Biomol NMR Assign 15, 449–453 (2021). https://doi.org/10.1007/s12104-021-10044-5
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DOI: https://doi.org/10.1007/s12104-021-10044-5