Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor

被引：0
|
作者：
Yan Li
Hui Qi Ng
Anna Ngo
Shuang Liu
Yih Wan Tan
Perlyn Zekui Kwek
Alvin W. Hung
Joma Joy
Jeffrey Hill
Thomas H. Keller
CongBao Kang
机构：
[1] Agency for Science,Experimental Therapeutics Centre
[2] Technology and Research,undefined
来源：
Biomolecular NMR Assignments | 2017年 / 11卷
关键词：
NSD3; Methyltransferase; SET domain; Backbone assignment;
D O I：
暂无
中图分类号：
学科分类号：
摘要：
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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页码：225 / 229
页数：4
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