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黄病毒衣壳蛋白的独特结构特征:结构-功能关系的新见解。

Unique structural features of flaviviruses' capsid proteins: new insights on structure-function relationship.

机构信息

Institute of Medical Biochemistry Leopoldo de Meis (IBqM), Federal University of Rio de Janeiro (UFRJ), 21941-590, Rio de Janeiro, RJ, Brazil.

Institute of Medical Biochemistry Leopoldo de Meis (IBqM), Federal University of Rio de Janeiro (UFRJ), 21941-590, Rio de Janeiro, RJ, Brazil; Multiuser Center for Biomolecular Innovation (CMIB) and Department of Physics, Institute of Biosciences, Letters and Exact Sciences (IBILCE), São Paulo State University (UNESP), 15054-000, São José do Rio Preto, SP, Brazil.

出版信息

Curr Opin Virol. 2021 Apr;47:106-112. doi: 10.1016/j.coviro.2021.02.005. Epub 2021 Mar 12.

DOI:10.1016/j.coviro.2021.02.005
PMID:33721656
Abstract

The Flaviviridae family comprises important human pathogens, including Dengue, Zika, West Nile, Yellow Fever and Japanese Encephalitis viruses. The viral genome, a positive-sense single-stranded RNA, is packaged by a single protein, the capsid protein, which is a small and highly basic protein that form intertwined homodimers in solution. Atomic-resolution structures of four flaviviruses capsid proteins were solved either in solution by nuclear magnetic resonance spectroscopy, or after protein crystallization by X-ray diffraction. Analyses of these structures revealed very particular properties, namely (i) the predominance of quaternary contacts maintaining the structure; (ii) a highly electropositive surface throughout the protein; and (iii) a flexible helix (α1). The goal of this review is to discuss the role of these features in protein structure-function relationship.

摘要

黄病毒科包括重要的人类病原体,如登革热、寨卡、西尼罗河、黄热病和日本脑炎病毒。病毒基因组是一条正链单链 RNA,由一种单一的蛋白质,衣壳蛋白,包装而成。衣壳蛋白是一种小而高度碱性的蛋白质,在溶液中形成相互交织的同源二聚体。通过核磁共振波谱法在溶液中或通过 X 射线衍射法在蛋白质结晶后,解析了四种黄病毒衣壳蛋白的原子分辨率结构。对这些结构的分析揭示了非常特殊的性质,即(i)主要存在维持结构的四级接触;(ii)整个蛋白质表面高度带正电荷;和(iii)一个灵活的螺旋(α1)。这篇综述的目的是讨论这些特征在蛋白质结构-功能关系中的作用。

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