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

被引:0
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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
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NSD3; Methyltransferase; SET domain; Backbone assignment;
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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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