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DAP5的MIF4G结构域的结晶及初步X射线衍射分析

Crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5.

作者信息

Frank Filipp, Virgili Geneviève, Sonenberg Nahum, Nagar Bhushan

机构信息

Department of Biochemistry, McGill University, Montréal, Québec, Canada.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jan 1;66(Pt 1):15-9. doi: 10.1107/S1744309109044315. Epub 2009 Dec 25.

DOI:10.1107/S1744309109044315
PMID:20057060
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2805526/
Abstract

Death-associated protein 5 (DAP5) is a member of the eIF4G family of scaffolding proteins that mediate cap-independent translation initiation by recruiting the translational machinery to internal ribosomal entry sites (IRESs) on mRNA. The MIF4G domain of DAP5 directly interacts with the eukaryotic initiation factors eIF4A and eIF3 and enhances the translation of several viral and cellular IRESs. Here, the crystallization and preliminary X-ray diffraction analysis of the MIF4G domain of DAP5 is presented.

摘要

死亡相关蛋白5(DAP5)是支架蛋白eIF4G家族的成员,通过将翻译机制募集到mRNA上的内部核糖体进入位点(IRES)来介导不依赖帽的翻译起始。DAP5的MIF4G结构域直接与真核起始因子eIF4A和eIF3相互作用,并增强几种病毒和细胞IRES的翻译。本文介绍了DAP5的MIF4G结构域的结晶及初步X射线衍射分析。

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本文引用的文献

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Processing of X-ray diffraction data collected in oscillation mode.振荡模式下收集的X射线衍射数据的处理。
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The crystal structure of the C-terminal DAP5/p97 domain sheds light on the molecular basis for its processing by caspase cleavage.C 端 DAP5/p97 结构域的晶体结构揭示了其经半胱天冬酶切割加工的分子基础。
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The eIF4G homolog DAP5/p97 supports the translation of select mRNAs during endoplasmic reticulum stress.真核起始因子4G(eIF4G)同源物DAP5/p97在内质网应激期间支持特定mRNA的翻译。
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Regulation of poly(A)-binding protein through PABP-interacting proteins.通过多聚腺苷酸结合蛋白(PABP)相互作用蛋白对多聚腺苷酸结合蛋白的调控。
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Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints.通过同时应用实空间和倒易空间约束来改进大分子电子密度图。
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