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本文引用的文献

1
The nine C-terminal amino acids of the respiratory syncytial virus protein P are necessary and sufficient for binding to ribonucleoprotein complexes in which six ribonucleotides are contacted per N protein protomer.呼吸道合胞病毒蛋白P的九个C末端氨基酸对于与核糖核蛋白复合体的结合是必要且充分的,其中每个N蛋白原体接触六个核糖核苷酸。
J Gen Virol. 2007 Jan;88(Pt 1):196-206. doi: 10.1099/vir.0.82282-0.
2
Crystal structure of the rabies virus nucleoprotein-RNA complex.狂犬病病毒核蛋白-RNA复合物的晶体结构
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Structure of the vesicular stomatitis virus nucleoprotein-RNA complex.水泡性口炎病毒核蛋白-RNA复合物的结构
Science. 2006 Jul 21;313(5785):357-60. doi: 10.1126/science.1126953. Epub 2006 Jun 15.
4
The intrinsically disordered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded.麻疹病毒核蛋白内在无序的C末端结构域通过两个不同位点与磷蛋白的C末端结构域相互作用,并且主要保持未折叠状态。
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Hsp72 recognizes a P binding motif in the measles virus N protein C-terminus.热休克蛋白72(Hsp72)识别麻疹病毒核蛋白(N蛋白)C末端的一个P结合基序。
Virology. 2005 Jun 20;337(1):162-74. doi: 10.1016/j.virol.2005.03.035.
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Natively disordered proteins: functions and predictions.天然无序蛋白质:功能与预测
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UCSF Chimera--a visualization system for exploratory research and analysis.加州大学旧金山分校奇美拉——一个用于探索性研究与分析的可视化系统。
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Conformational flexibility in recombinant measles virus nucleocapsids visualised by cryo-negative stain electron microscopy and real-space helical reconstruction.通过冷冻负染电子显微镜和实空间螺旋重建可视化重组麻疹病毒核衣壳中的构象灵活性。
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The 12 A structure of trypsin-treated measles virus N-RNA.经胰蛋白酶处理的麻疹病毒N-RNA的12 A结构。
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10
The C-terminal domain of measles virus nucleoprotein belongs to the class of intrinsically disordered proteins that fold upon binding to their physiological partner.麻疹病毒核蛋白的C末端结构域属于内在无序蛋白类别,这类蛋白在与它们的生理伴侣结合时会发生折叠。
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呼吸道合胞病毒核衣壳蛋白-RNA十聚体环的24埃结构

The 24-angstrom structure of respiratory syncytial virus nucleocapsid protein-RNA decameric rings.

作者信息

Maclellan Kirsty, Loney Colin, Yeo R Paul, Bhella David

机构信息

Medical Research Council Virology Unit, Institute of Virology, Church Street, Glasgow G11 5JR, United Kingdom.

出版信息

J Virol. 2007 Sep;81(17):9519-24. doi: 10.1128/JVI.00526-07. Epub 2007 Jun 13.

DOI:10.1128/JVI.00526-07
PMID:17567697
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1951410/
Abstract

Respiratory syncytial virus (RSV), a nonsegmented, negative-sense RNA-containing virus, is a common cause of lower respiratory tract disease. Expression of RSV nucleocapsid protein (N) in insect cells using the baculovirus expression system leads to the formation of N-RNA complexes that are morphologically indistinguishable from viral nucleocapsids. When imaged in an electron microscope, three distinct types of structures were observed: tightly wound short-pitch helices, highly extended helices, and rings. Negative stain images of N-RNA rings were used to calculate a three-dimensional reconstruction at 24 A resolution, revealing features similar to those observed in nucleocapsids from other viruses of the order Mononegavirales. The reconstructed N-RNA rings comprise 10 N monomers and have an external radius of 83 A and an internal radius of 40 A. Comparison of this structure with crystallographic data from rabies virus and vesicular stomatitis virus N-RNA rings reveals striking morphological similarities.

摘要

呼吸道合胞病毒(RSV)是一种无节段、含负链RNA的病毒,是下呼吸道疾病的常见病因。利用杆状病毒表达系统在昆虫细胞中表达RSV核衣壳蛋白(N),会导致形成N-RNA复合物,其形态与病毒核衣壳无法区分。在电子显微镜下成像时,观察到三种不同类型的结构:紧密缠绕的短螺距螺旋、高度伸展的螺旋和环。利用N-RNA环的负染图像以24埃分辨率计算三维重建,揭示出与从单股负链RNA病毒目其他病毒的核衣壳中观察到的特征相似的特征。重建的N-RNA环由10个N单体组成,外半径为83埃,内半径为40埃。将该结构与狂犬病病毒和水疱性口炎病毒N-RNA环的晶体学数据进行比较,发现了惊人的形态学相似性。