Abstract
NSD3 is a histone H3 methyltransferase that plays an important role in chromatin biology. A construct containing the methyltransferase domain encompassing residues Q1049-K1299 of human NSD3 was obtained and biochemical activity was demonstrated using histone as a substrate. Here we report the backbone HN, N, Cα, C′, and side chain Cβ assignments of the construct in complex with S-adenosyl-l-methionine (SAM). Based on these assignments, secondary structures of NSD3/SAM complex in solution were determined.
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Acknowledgements
CK appreciates the support from A*STAR JCO Grant (1431AFG102/1331A028). We also thank Prof Ho Sup Yoon and Dr. Hong Ye from Nanyang Technological University for the help of NMR experiments.
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Li, Y., Ng, H.Q., Ngo, A. et al. Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor. Biomol NMR Assign 11, 225–229 (2017). https://doi.org/10.1007/s12104-017-9753-8
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DOI: https://doi.org/10.1007/s12104-017-9753-8