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. 2016 Oct;10(2):315-20.
doi: 10.1007/s12104-016-9691-x. Epub 2016 Jun 29.

NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2

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NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2

Nader Amin et al. Biomol NMR Assign. 2016 Oct.

Abstract

Proteins of the NSD family are histone-methyl transferases with critical functions in the regulation of chromatin structure and function. NSD1 and NSD2 are homologous proteins that function as epigenetic regulators of transcription through their abilities to catalyse histone methylation. Misregulation of NSD1 and NSD2 expression or mutations in their genes are linked to a number of human diseases such as Sotos syndrome, and cancers including acute myeloid leukemia, multiple myeloma, and lung cancer. The catalytic domain of both proteins contains a conserved SET domain which is involved in histone methylation. Here we report the backbone resonance assignments and secondary structure information of the catalytic domains of human NSD1 and NSD2.

Keywords: Histone-methyl transferase; MMSET; NMR resonance assignments; NMR stability screen; NSD family; NSD1; NSD2; Nuclear receptor-binding SET domain; WHSC1.

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