STRUCTURAL SIMILARITY BETWEEN THE P17 MATRIX PROTEIN OF HIV-1 AND INTERFERON-GAMMA
STRUCTURAL SIMILARITY BETWEEN THE P17 MATRIX PROTEIN OF HIV-1 AND INTERFERON-GAMMA
复制标题
DOI：
10.1038/370666a0
复制
发表时间：
1994-08-25
期刊：
影响因子：
64.8
通讯作者：
CAMPBELL, I
中科院分区：
文献类型：
--
作者：
MATTHEWS, S;BARLOW, P;CAMPBELL, I
人类免疫缺陷病毒（HIV）基质蛋白，p17，形成病毒核心的外壳，衬在病毒膜的内表面（1-4）。蛋白质有几个关键功能。它通过将gag前体多蛋白p55引导至宿主细胞膜的靶向信号来协调病毒组装（1，5 -7），并且它与跨膜蛋白gp 41相互作用以将env编码的蛋白保留在病毒中（8）。此外，p17含有一个核定位信号，可将整合前复合物引导至感染细胞的细胞核（9）。这使得病毒能够感染非分裂细胞，这是HIV和其他慢病毒的显著特征。我们已经确定了解决方案的结构p17的核磁共振（NMR）的均方根偏差为0.9埃的明确定义的区域的骨干。它由四个由短环连接的螺旋和一个不规则的混合β-片层组成，β-片层提供了一个带正电荷的表面，用于与膜的内层相互作用。螺旋拓扑结构是不寻常的;布鲁克海文蛋白质数据库只包含一个类似的结构，即免疫调节剂干扰素-γ。
THE human immunodeficiency virus (HIV) matrix protein, p17, Forms the outer shell of the core of the virus, lining the inner surface of the viral membrane(1-4). The protein has several key functions. It orchestrates viral assembly via targeting signals that direct the gag precursor polyprotein, p55, to the host cell membrane(1,5-7) and it interacts with the transmembrane protein, gp41, to retain the env-encoded proteins in the virus(8). In addition, p17 contains a nuclear localization signal that directs the preintegration complex to the nucleus of infected cells(9). This permits the virus to infect productively non-dividing cells, a distinguishing feature of HIV and other lentiviruses. We have determined the solution structure of p17 by nuclear magnetic resonance (NMR) with a root-mean square deviation for the backbone of the well-defined regions of 0.9 Angstrom. It consists of four helices connected by short loops and an irregular, mixed beta-sheet which provides a positively charged surface for interaction with the inner layer of the membrane. The helical topology is unusual; the Brookhaven protein database contains only one similar structure, that of the immune modulator interferon-gamma.