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
中科院分区:
文献类型:
--
作者:
Sugrue RJ;Hay AJ
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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