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Crystal Structure of the Human SUV39H1 Chromodomain and Its Recognition of Histone H3K9me2/3

Crystal Structure of the Human SUV39H1 Chromodomain and Its Recognition of Histone H3K9me2/3

Tao Wang, Chao Xu, Yanli Liu, Kai Fan, Zhihong Li, Xing Sun, Hui Ouyang, Xuecheng Zhang, Jiahai Zhang, Yanjun Li, Farrell Mackenzie, Jinrong Min, Xiaoming Tu

PLoS One. 2012;7(12):e52977.

PMID: 23285239

Abstract:

SUV39H1, the first identified histone lysine methyltransferase in human, is involved in chromatin modification and gene regulation. SUV39H1 contains a chromodomain in its N-terminus, which potentially plays a role in methyl-lysine recognition and SUV39H1 targeting. In this study, the structure of the chromodomain of human SUV39H1 was determined by X-ray crystallography. The SUV39H1 chromodomain displays a generally conserved structure fold compared with other solved chromodomains. However, different from other chromodomains, the SUV39H1 chromodomain possesses a much longer helix at its C-terminus. Furthermore, the SUV39H1 chromodomain was shown to recognize histone H3K9me2/3 specifically.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42416094	SUV39H1 human			Price

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