Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel.

Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel.
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DOI:
10.1016/0042-6822(91)90075-m
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发表时间:
1991-03
期刊:
影响因子:
3.7
通讯作者:
Hay AJ
Hay AJ
中科院分区:
医学3区
文献类型:
--
作者:
Sugrue RJ;Hay AJ

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证据表明,甲型流感病毒的M2蛋白在感染细胞中以同源四聚体的形式存在,由两个二硫键连接的二聚体通过非共价相互作用结合在一起。跨膜α-螺旋结构域的两亲性与形成跨膜通道的蛋白质一致,特异性抗甲型流感药物金刚烷胺与该蛋白质相互作用。这些特征共同为以下假设提供了结构基础:M2具有能够调节反式高尔基体网络囊泡pH值的质子易位功能,这是促进血凝素糖蛋白正确成熟的重要作用。
The evidence presented shows that the M2 protein of influenza A viruses exists in infected cells as a homotetramer composed of two disulfide-linked dimers held together by noncovalent interactions. The amphiphilic nature of the transmembrane α-helical domain is consistent with the protein forming a transmembrane channel with which amantadine, the specific anti-influenza A drug, interacts. Together these features provide a structural basis for the hypothesis that M2 has a proton translocation function capable of regulating the pH of vesicles of the trans-Golgi network, a role important in promoting the correct maturation of the hemagglutinin glycoprotein.
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