STRUCTURAL CHARACTERIZATION OF ESCHERICHIA COLI HSP90 HOMOLOGUE

大肠杆菌 HSP90 同源物的结构表征

• 批准号: 6119493
• 负责人: ANDREW K SHIAU
• 金额: --
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-04-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6119493
• 关键词: biomaterials; genome

The 90 kDa heat shock protein (hsp90) is a highly abundant, highly conserved protein in both prokaryotes and eukaryotes. Like several other heat shock proteins, hsp90 has been shown to chaperone protein folding in vitro. In addition, hsp90 modulates the activities of a variety of signal transduction molecules including steroid hormone receptors as well as nonreceptor tyrosine kinases (such as v-src). Overall, the studies of the interactions between hsp90 and these signal transduction molecules hint that the mechanism through which hsp90 modulates the functions of these molecules and its role as a chaperone may overlap; these signaling molecules may have co-opted the ability of hsp90 to stabilize folding intermediates into regulating conformational changes necessary for signaling. Therefore, we have initiated a structural study of htpG, the E. coli member of the hsp90 family.

90 kDa 热休克蛋白 (hsp90) 是一种高丰度、高度 原核生物和真核生物中的保守蛋白质。 像几个 其他热休克蛋白，hsp90 已被证明是伴侣蛋白 体外折叠。 此外，hsp90 还调节 多种信号转导分子，包括类固醇激素 受体以及非受体酪氨酸激酶（例如 v-src）。 总体而言，hsp90 与这些物质之间相互作用的研究 信号转导分子暗示其机制 hsp90 调节这些分子的功能及其作为 伴侣可能会重叠；这些信号分子可能已经选择了 hsp90稳定折叠中间体进入调节的能力 信号传导所必需的构象变化。 因此，我们有 启动了 htpG（hsp90 的大肠杆菌成员）的结构研究 家庭。