The active site of the SET domain is constructed on a knot
The active site of the SET domain is constructed on a knot
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DOI：
10.1038/nsb861
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发表时间：
2002-11-01
期刊：
影响因子：
--
通讯作者：
Khorasanizadeh, S
中科院分区：
文献类型：
--
作者：
Jacobs, SA;Harp, JM;Khorasanizadeh, S
SET结构域包含赖氨酸甲基转移酶的催化中心，它以组蛋白的N末端为靶标，调节染色质功能。在这里，我们报道了在没有和存在辅因子产物S-腺苷-L-同型半胱氨酸(ADOHcy)的情况下，Set7/9蛋白的结构。SET结构域中的一个结有助于形成甲基转移酶活性位点，在那里ADOHcy结合，赖氨酸甲基化可能发生。对SET蛋白家族中的序列进行结构指导的比较表明，结亚基结构和活性位点环境是SET结构域的保守特征。
The SET domain contains the catalytic center of lysine methyltransferases that target the N-terminal tails of histones and regulate chromatin function. Here we report the structure of the SET7/9 protein in the absence and presence of its cofactor product, S-adenosyl-L-homocysteine (AdoHcy). A knot within the SET domain helps form the methyltransferase active site, where AdoHcy binds and lysine methylation is likely to occur. A structure-guided comparison of sequences within the SET protein family suggests that the knot substructure and active site environment are conserved features of the SET domain.