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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Solution structure of dengue virus capsid protein reveals another fold
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Solution structure of dengue virus capsid protein reveals another fold

机译:登革病毒衣壳蛋白的溶液结构揭示了另一折叠

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Dengue virus is responsible for approximate to50-100 million infections, resulting in nearly 24,000 deaths annually. The capsid (C) protein of dengue virus is essential for specific encapsidation of the RNA genome, but little structural information on the C protein is available. We report the solution structure of the 200-residue homodimer of dengue 2 C protein. The structure provides, to our knowledge, the first 3D picture of a flavivirus C protein and identifies a fold that includes a large dimerization surface contributed by two pairs of helices, one of which has characteristics of a coiled-coil. NMR structure determination involved a secondary structure sorting approach to facilitate assignment of the inter-subunit nuclear Overhauser effect interactions. The dimer of dengue C protein has an unusually high net charge, and the structure reveals an asymmetric distribution of basic residues over the surface of the protein. Nearly half of the basic residues lie along one face of the dimer. In contrast, the conserved hydrophobic region forms an extensive apolar surface at a dimer interface on the opposite side of the molecule. We propose a model for the interaction of dengue C protein with RNA and the viral membrane that is based on the asymmetric charge distribution of the protein and is consistent with previously reported results. [References: 33]
机译:登革热病毒造成大约50-100百万例感染,每年导致近24,000人死亡。登革病毒的衣壳(C)蛋白对于RNA基因组的特异性衣壳化至关重要,但是有关C蛋白的结构信息很少。我们报告了登革热2 C蛋白的200残基同型二聚体的溶液结构。据我们所知,该结构提供了黄病毒C蛋白的第一张3D图片,并鉴定出包含由两对螺旋构成的大二聚化表面的折叠,其中两个螺旋具有卷曲螺旋的特征。 NMR结构确定涉及二级结构分类方法,以促进亚单位间核Overhauser效应相互作用的分配。登革热C蛋白的二聚体具有异常高的净电荷,其结构揭示了蛋白表面碱性残基的不对称分布。几乎一半的碱性残基位于二聚体的一个面上。相反,保守的疏水区在分子相对侧的二聚体界面处形成了广泛的非极性表面。我们提出了一种基于蛋白质的不对称电荷分布的登革热C蛋白与RNA和病毒膜相互作用的模型,该模型与先前报道的结果一致。 [参考:33]

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