CRYSTAL STRUCTURE OF MOLECULAR CHAPERONE

分子伴侣的晶体结构

• 批准号: 6586751
• 负责人: LARRY E VICKERY
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586751
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; proteins; radiography; structural biology

Molecular chaperones play key roles in protein folding, transport across membranes, and in response to stressful stimuli. We have recently succeeded in overexpressing, purifying and crystallizing Hsc20, a J-motif co-chaperone protein which regulates the chaperone Hsc66 in E. coli. A native data set to 1.9 E resolution has been collected, and heavy atom derivatives are now being characterized in order to solve the structure by multiple isomorphous replacement methods.

分子伴侣在蛋白质折叠、运输中起着关键作用 跨膜，并对应激刺激做出反应。我们有 最近成功地过度表达、纯化和结晶 Hsc20，一个J-基序的伴侣蛋白，调节伴侣 Hsc66在大肠杆菌中的表达。设置为1.9E分辨率的原生数据集 收集到的，重原子衍生品现在正在 用多重同构替换法解结构 方法：研究方法。