STRUCTURAL STUDIES OF VPU IN PHOSPHOLIPID MONOLAYERS AND BILAYERS

我们计划研究HIV-1辅助蛋白的结构 面向矢量的单膜系统中的VPU利用 基于同步辐射的最新X射线散射和冷 中子散射技术。第二、第四纪 VPU跨膜区结构，包括VPU跨膜区的位置 该结构域中的钾离子，以及三级结构 VPU的细胞质结构域，包括后者对 Ser52和Ser56残基ITS的磷酸化将是特别重要的 利息。因为跨膜结构域及其相关的 单价阳离子通道活性是病毒增强的原因 从细胞表面和它的细胞质区域释放负责 依赖于磷酸化的诱导降解 HIV受体CD$，拟议的结构研究有望 对VPU的两种机制提供了实质性的见解 参与艾滋病毒-1感染过程的独立行动。在……里面 此外，通过确定跨膜的结构起源 DOMAIN的通道活性，药物干预的潜在靶点 基于VPU特异性通道阻滞剂的开发 如果是这样的话。

Well plan to investigate the structure of the HIV-1 accessory protein Vpu within vectorially-oriented single membrane systems utilizing state-of-the-art synchrotron radiation-based x-ray scattering and cold neutron scattering techniques. The secondary and quaternary structures of Vpu's transmembrane domain, including the locations of potassium cations within this domain, and the tertiary structure of Vpu's cytoplasmic domain, including the latter's dependence on the phosphorylation of its of Ser52 and Ser56 residues, will be of particular interest. Since the transmembrane domain and its associated monovalent cation channel activity are responsible for enhancing virus release from the cell surface and its cytoplasmic domain is responsible for the phosphorylation-dependent induction of degradation of the HIV receptor CD$, the structural studies proposed are expected to provide substantial insight into the mechanism of Vpu's two independent actions involved in the course of HIV-1 infection. In addition, by so-determining the structural origin of the transmembrane domain's channel activity, a potential target for drug intervention based on the development of Vpu-specific channel blockers would be provided.