Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly
Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: Implications for membrane association and assembly
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DOI：
10.1073/pnas.93.7.3099
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发表时间：
1996-04-02
影响因子：
11.1
通讯作者：
Sundquist, WI
中科院分区：
文献类型：
--
作者：
Hill, CP;Worthylake, D;Sundquist, WI
人类免疫缺陷病毒 1 型 (HIV-1) 基质蛋白形成与病毒内膜相关的结构外壳，并在整个病毒生命周期中发挥其他重要功能。以 2.3 埃分辨率测定的 HIV-1 基质蛋白的晶体结构表明，各个基质分子由五个主要螺旋组成，其顶部有一个三链混合 β 折叠。出乎意料的是，该蛋白质在三种不同的晶格中组装成三聚体，在三聚体界面处埋藏了 1880 埃 (2) 的可及表面积。三聚化似乎产生了一个大的二分膜结合表面，其中暴露的碱性残基可以与N端肉豆蔻酰基基团合作，将蛋白质锚定在病毒的酸性内膜上。
The human immunodeficiency virus type 1 (HIV-1) matrix protein forms a structural shell associated with the inner viral membrane and performs other essential functions throughout the viral life cycle, The crystal structure of the HIV-1 matrix protein, determined at 2.3 Angstrom resolution, reveals that individual matrix molecules are composed of five major helices capped by a three-stranded mixed beta-sheet. Unexpectedly, the protein assembles into a trimer in three different crystal lattices, burying 1880 Angstrom(2) of accessible surface area at the trimer interfaces. Trimerization appears to create a large, bipartite membrane binding surface in which exposed basic residues could cooperate with the N-terminal myristoyl groups to anchor the protein on the acidic inner membrane of the virus.