Backbone resonance assignments for the SET domain of the human methyltransferase NSD2

Romel Bobby; Karolina Peciak; Alexander G Milbradt

doi:10.1007/s12104-016-9689-4

Backbone resonance assignments for the SET domain of the human methyltransferase NSD2

Biomol NMR Assign. 2016 Oct;10(2):307-10. doi: 10.1007/s12104-016-9689-4. Epub 2016 Jul 1.

Authors

Romel Bobby¹, Karolina Peciak¹, Alexander G Milbradt²

Affiliations

¹ Discovery Sciences, Innovative Medicines and Early Development Biotech Unit, AstraZeneca, Alderley Park, SK10 4TG, UK.
² Discovery Sciences, Innovative Medicines and Early Development Biotech Unit, AstraZeneca, Alderley Park, SK10 4TG, UK. Alex.Milbradt@astrazeneca.com.

PMID: 27368234
DOI: 10.1007/s12104-016-9689-4

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 [Formula: see text], N, C[Formula: see text], [Formula: see text] and side-chain [Formula: see text] assignments of a 25 kDa NSD2 SET domain construct, spanning residues 991-1203. A chemical shift analysis of C[Formula: see text], [Formula: see text] and [Formula: see text] resonances predicts a secondary structural pattern that is in agreement with homology models.

Keywords: Backbone assignment; MMSET; NSD2; SET domain.

MeSH terms

Histone-Lysine N-Methyltransferase / chemistry*
Humans
Nuclear Magnetic Resonance, Biomolecular*
Protein Domains
Protein Structure, Secondary
Repressor Proteins / chemistry*

Substances

Repressor Proteins
Histone-Lysine N-Methyltransferase
NSD2 protein, human