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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure analysis of the conserved methyltransferase domain of human trimethylguanosine synthase TGS1
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Structure analysis of the conserved methyltransferase domain of human trimethylguanosine synthase TGS1

机译:结构分析的守恒的甲基转移酶域的人类trimethylguanosine合成酶TGS1

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摘要

Methyltransferases play an important role in the post-transcriptional maturation of most ribonucleic acids. The modification of spliceosomal UsnRNAs includes N2-dimethyl-ation of the m~7G cap catalyzed by trimethylguanosine synthase 1 (TGS1). This 5'-cap hypermethylation occurs during the biogenesis of UsnRNPs as it initiates the m_3G cap-dependent nuclear import of UsnRNPs. The conserved methyltransferase domain of human TGS1 has been purified, crystallized and the crystal structure of this domain with bound substrate m~7GpppA was solved by means of multiple-wavelength anomalous dispersion.
机译:甲基转移酶起着重要的作用转录后的成熟核醣核酸酸。spliceosomal UsnRNAs包括N2-dimethyl-ation的m ~ 7 g帽trimethylguanosine催化合酶1 (TGS1)。发生在UsnRNPs生物起源的发起m_3G帽依赖核进口UsnRNPs。域的人类TGS1纯化,结晶的晶体结构域名绑定衬底m ~ 7 gpppa是解决通过对多波长反常分散。

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