Backbone Resonance Assignments for the SET Domain of the Human Methyltransferase NSD2

Romel Bobby, Karolina Peciak, Alexander G Milbradt

Biomol NMR Assign. 2016 Oct;10(2):307-10.

PMID: 27368234

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.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
IAR42416099 NSD2 catalytic domain Active human NSD2 catalytic domain Active human Price
qrcode
Privacy Policy | Cookie Policy | Copyright © 2024 Alfa Chemistry. All rights reserved.