Matthews S, Barlow P, Boyd J, Barton G, Russell R, Mills H, Cunningham M, Meyers N, Burns N, Clark N
Department of Biochemistry, University of Oxford, UK.
Nature. 1994 Aug 25;370(6491):666-8. doi: 10.1038/370666a0.
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. 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 and it interacts with the transmembrane protein, gp41, to retain the env-encoded proteins in the virus. In addition, p17 contains a nuclear localization signal that directs the preintegration complex to the nucleus of infected cells. 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 A. 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.
人类免疫缺陷病毒（HIV）基质蛋白p17构成病毒核心的外壳，位于病毒膜的内表面。该蛋白具有多种关键功能。它通过靶向信号协调病毒组装，这些信号将gag前体多蛋白p55导向宿主细胞膜，并且它与跨膜蛋白gp41相互作用，以将env编码的蛋白保留在病毒中。此外，p17包含一个核定位信号，该信号将整合前复合物导向受感染细胞的细胞核。这使得病毒能够有效感染非分裂细胞，这是HIV和其他慢病毒的一个显著特征。我们通过核磁共振（NMR）确定了p17的溶液结构，其明确区域主链的均方根偏差为0.9埃。它由四个通过短环连接的螺旋和一个不规则的混合β折叠组成，该β折叠为与膜内层的相互作用提供了一个带正电荷的表面。螺旋拓扑结构不寻常；布鲁克海文蛋白质数据库中只有一种类似结构，即免疫调节剂干扰素-γ的结构。
