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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of the JmjC-domain-containing protein JMJD5
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Structure of the JmjC-domain-containing protein JMJD5

机译:JmjC-domain-containing蛋白质的结构

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摘要

The post-translational modification of histone tails is the principal process controlling epigenetic regulation in eukaryotes. The lysine methylation of histones is dynamically regulated by two distinct classes of enzymes: methyltransferases and demethylases. JMJD5, which plays an important role in cell-cycle progression, circadian rhythms and embryonic cell proliferation, has been shown to be a JmjC-domain-containing histone demethylase with enzymatic activity towards H3K36me2. Here, the crystal structure of human JMJD5 lacking the N-terminal 175 amino-acid residues is reported. The structure showed that the Gln275, Trp310 and Trp414 side chains might block the insertion of methylated lysine into the active centre of JMJD5, suppressing the histone demethylase activity of the truncated JMJD5 construct. A comparison of the structure of JMJD5 with that of FIH, a well characterized protein hydroxylase, revealed that human JMJD5 might function as a protein hydroxylase. The interaction between JMJD5 and the core histone octamer proteins indicated that the histone proteins could be potential substrates for JMJD5.
机译:组蛋白的翻译后修饰反面是校长的过程控制表观遗传调控在真核生物。组蛋白的甲基化是动态监管通过两个不同的类的酶:甲基转移酶和demethylases。在细胞循环中扮演一个重要的角色进展,昼夜节律和胚胎细胞扩散,已被证明是一个JmjC-domain-containing组蛋白demethylase与对H3K36me2酶活性。人类JMJD5缺乏的晶体结构氨基端175个氨基酸残基。结构表明,Gln275, Trp310和Trp414侧链可能块的插入甲基化赖氨酸的活动中心JMJD5,抑制组蛋白demethylase截断JMJD5构造的活动。JMJD5与结构的比较富士康,特征蛋白羟化酶,表明人类JMJD5可能作为一个函数羟化酶蛋白质。JMJD5和核心蛋白质组蛋白八聚物表明组蛋白的蛋白质潜在的JMJD5基质。

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