与辅因子结合的人类甲基转移酶NSD3的SET结构域的主链共振归属
Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor.
作者信息
Li Yan, Ng Hui Qi, Ngo Anna, Liu Shuang, Tan Yih Wan, Kwek Perlyn Zekui, Hung Alvin W, Joy Joma, Hill Jeffrey, Keller Thomas H, Kang CongBao
机构信息
Experimental Therapeutics Centre, Agency for Science, Technology and Research, 31 Biopolis Way Nanos, #03-01, Singapore, 138669, Singapore.
出版信息
Biomol NMR Assign. 2017 Oct;11(2):225-229. doi: 10.1007/s12104-017-9753-8. Epub 2017 Aug 14.
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.
NSD3是一种组蛋白H3甲基转移酶，在染色质生物学中发挥重要作用。我们获得了一个包含人NSD3第1049位谷氨酰胺至1299位赖氨酸残基的甲基转移酶结构域的构建体，并以组蛋白为底物证明了其生化活性。本文报道了该构建体与S-腺苷-L-甲硫氨酸（SAM）复合物的主链HN、N、Cα、C'以及侧链Cβ的化学位移归属。基于这些归属，确定了溶液中NSD3/SAM复合物的二级结构。
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