来自HIV-1 gp41的ectodomain的原子结构
W Weissenhorn1, A Dessen, S C Harrison
1Laboratory of Molecular Medicine, The Children's Hospital, Boston, Massachusetts 02215, USA.
Nature
|May 22, 1997
概括
对HIV-1 gp41ectodomain的结构分析揭示了一个三链的α-螺旋螺旋卷轴核心. 这种由X射线晶体学确定的结构表明一种常见的病毒膜融合机制.
科学领域:
- 结构生物学 结构生物学
- 病毒学 病毒学
- 分子生物学分子生物学
背景情况:
- 人类免疫缺陷病毒1型 (HIV-1) 进入宿主细胞是由包膜糖蛋白复合体gp120/gp41介导的.
- 在与CD4和共受体结合时,gp120/gp41复合体经历了构造变化,从而启动了膜融合.
研究的目的:
- 为了确定HIV-1 gp41 ectodomain的蛋白酶耐药片段的三维结构.
- 为了阐明病毒膜融合的结构基础.
主要方法:
- 使用X射线结晶学来确定gp41ectodomain的结构.
- 在gp41 ectodomain的溶解过程中,使用三元基 GCN4 绕线圈代替了融合.
主要成果:
- gp41 ectodomain 碎片的核心结构是一个延伸的,三链的α-螺旋螺旋卷轴.
- 氨基末端位于螺旋线圈的尖端.
- 一个碳氧终端的α螺旋螺旋反向地与卷轴的卷轴打包在一起,使终端结合在一起.
结论:
- 确定的结构为HIV-1膜融合的机制提供了洞察力.
- 与其他病毒融合蛋白的结构相似性表明,不同病毒的融合启动机制是保留的.
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