Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation.
Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation.
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副粉状蛋白在其亚稳态的预融合构象中的结构。
DOI：
10.1038/nature04322
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发表时间：
2006-01-05
期刊：
影响因子：
64.8
通讯作者：
Jardetzky TS
中科院分区：
文献类型：
--
作者：
Yin HS;Wen X;Paterson RG;Lamb RA;Jardetzky TS
包膜病毒进化出复杂的糖蛋白机制，驱动病毒和细胞膜的融合，允许病毒基因组进入细胞。对于副粘病毒，融合（F）蛋白催化该膜合并和进入步骤，并且已经假定F蛋白在该过程中经历复杂的重折叠。在这里，我们报告的晶体结构的副流感病毒5 F蛋白在其融合前的构象，通过添加一个羧基末端三聚化结构域稳定。F蛋白的结构表明，融合前和融合后状态之间存在深刻的构象差异，涉及二级和三级结构的转换。融合机制的关键部分，包括疏水性融合肽和两个螺旋七肽重复区的位置和结构转换，阐明了F蛋白介导的膜融合机制。本文的在线版本（doi：10.1038/nature 04322）包含补充材料，可供授权用户使用。被包膜病毒如流感病毒、HIV和副粘病毒感染的细胞需要病毒和细胞膜的融合。参与这一过程的许多病毒蛋白是高度专业化的。起初，它们采用亚稳态形状，储存进入细胞所需的能量，然后蛋白质形状的不可逆变化催化膜融合。融合前副流感病毒5 F融合蛋白的晶体结构现已确定。融合前和融合后状态之间的广泛差异揭示了膜融合机制的细节，这对于开发预防病毒感染的新方法可能具有价值。本文的在线版本（doi：10.1038/nature 04322）包含补充材料，可供授权用户使用。
Enveloped viruses have evolved complex glycoprotein machinery that drives the fusion of viral and cellular membranes, permitting entry of the viral genome into the cell. For the paramyxoviruses, the fusion (F) protein catalyses this membrane merger and entry step, and it has been postulated that the F protein undergoes complex refolding during this process. Here we report the crystal structure of the parainfluenza virus 5 F protein in its prefusion conformation, stabilized by the addition of a carboxy-terminal trimerization domain. The structure of the F protein shows that there are profound conformational differences between the pre- and postfusion states, involving transformations in secondary and tertiary structure. The positions and structural transitions of key parts of the fusion machinery, including the hydrophobic fusion peptide and two helical heptad repeat regions, clarify the mechanism of membrane fusion mediated by the F protein. The online version of this article (doi:10.1038/nature04322) contains supplementary material, which is available to authorized users. Infection of a cell by enveloped viruses such as influenza, HIV and paramyxoviruses requires the fusion of viral and cellular membranes. Many of the viral proteins involved in this process are highly specialized. At first they adopt a metastable shape that stores the energy needed for entry into cells, then irreversible changes in the protein shape catalyse membrane fusion. The crystal structure of pre-fusion parainfluenza virus 5 F fusion protein has now been determined. The extensive differences between pre- and post-fusion states reveal details of the mechanism of membrane fusion which could be of value for developing novel approaches to preventing viral infections. The online version of this article (doi:10.1038/nature04322) contains supplementary material, which is available to authorized users.
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影响因子：
56.9
作者：
HARBURY, PB;ZHANG, T;ALBER, T
通讯作者：
ALBER, T
影响因子：
5.4
作者：
Chen, B;Cheng, YF;Wiley, DC
通讯作者：
Wiley, DC
影响因子：
64.8
作者：
HARBURY, PB;KIM, PS;ALBER, T
通讯作者：
ALBER, T
DOI：
10.1083/jcb.151.2.413
发表时间：
2000-10-16
期刊：
The Journal of cell biology
影响因子：
--
作者：
Melikyan GB;Markosyan RM;Hemmati H;Delmedico MK;Lambert DM;Cohen FS
通讯作者：
Cohen FS
DOI：
10.1038/nsb0498-276
发表时间：
1998-04-01
期刊：
NATURE STRUCTURAL BIOLOGY
影响因子：
--
作者：
Furuta, RA;Wild, CT;Weiss, CD
通讯作者：
Weiss, CD