Abstract
Aberrant NSD2 methyltransferase activity is implicated as the oncogenic driver in multiple myeloma, suggesting opportunities for novel therapeutic intervention. The methyltransferase activity of NSD2 resides in its catalytic SET domain, which is conserved among most lysine methyltransferases. Here we report the backbone \(\hbox {H}^{\mathrm{N}}\), N, C\(^{\prime }\), \(\hbox {C}^\alpha\) and side-chain \(\hbox {C}^\beta\) assignments of a 25 kDa NSD2 SET domain construct, spanning residues 991–1203. A chemical shift analysis of C\(^{\prime }\), \(\hbox {C}^\alpha\) and \(\hbox {C}^\beta\) resonances predicts a secondary structural pattern that is in agreement with homology models.
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Acknowledgments
We would like to thank Dr. Paul Wan for discussions around protein expression and purification and Dr. Martin Packer for providing the homology model of NSD2 SET domain. We are grateful to Dr. Kevin Embrey for reading the manuscript prior to submission.
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Bobby, R., Peciak, K. & Milbradt, A.G. Backbone resonance assignments for the SET domain of the human methyltransferase NSD2. Biomol NMR Assign 10, 307–310 (2016). https://doi.org/10.1007/s12104-016-9689-4
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DOI: https://doi.org/10.1007/s12104-016-9689-4