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病毒入侵的结构基础:副粘病毒F蛋白的启示

Structural basis of viral invasion: lessons from paramyxovirus F.

作者信息

Lamb Robert A, Jardetzky Theodore S

机构信息

Department of Biochemistry, Molecular Biology, Cell Biology, Northwestern University, Evanston, IL 60208, USA.

出版信息

Curr Opin Struct Biol. 2007 Aug;17(4):427-36. doi: 10.1016/j.sbi.2007.08.016. Epub 2007 Sep 17.

Abstract

The structures of glycoproteins that mediate enveloped virus entry into cells have revealed dramatic structural changes that accompany membrane fusion and provided mechanistic insights into this process. The group of class I viral fusion proteins includes the influenza hemagglutinin, paramyxovirus F, HIV env, and other mechanistically related fusogens, but these proteins are unrelated in sequence and exhibit clearly distinct structural features. Recently determined crystal structures of the paramyxovirus F protein in two conformations, representing pre-fusion and post-fusion states, reveal a novel protein architecture that undergoes large-scale, irreversible refolding during membrane fusion, extending our understanding of this diverse group of membrane fusion machines.

摘要

介导包膜病毒进入细胞的糖蛋白结构揭示了伴随膜融合的显著结构变化,并为这一过程提供了机制上的见解。I类病毒融合蛋白包括流感血凝素、副粘病毒F、HIV包膜蛋白以及其他机制相关的融合蛋白,但这些蛋白在序列上无关,且具有明显不同的结构特征。最近确定的处于两种构象(代表融合前和融合后状态)的副粘病毒F蛋白的晶体结构,揭示了一种新型蛋白质结构,该结构在膜融合过程中经历大规模、不可逆的重折叠,扩展了我们对这一多样的膜融合机器群体的理解。

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