CRYSTAL STRUCTURE OF MOLECULAR CHAPERONE, HSC20

分子伴侣 HSC20 的晶体结构

• 批准号: 6437542
• 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: 2001
• 资助国家: 美国
• 起止时间: 2001-03-01 至 2002-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6437542
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; human tissue; proteins; radiography; structural biology; bioimaging /biomedical imaging; biomaterials; biomedical resource; human tissue; proteins; radiography; structural biology

Molecular chaperones play key roles in protein folding, transport across membranes, and in response to stressful stimuli. Hsc20 is a DnaJ-type "co-chaperone" protein encoded in a recently discovered operon in E. coli which also encodes a DnaK/hsp70-type chaperone. To date, no structure for a DnaJ co-chaperone has been determined. We have recently succeeded in overexpresing, purifying and crystallizing Hsc20. Thus, Hsc20 could provide the first complete high resolution crystal structure for proteins of this class.

分子伴侣在蛋白质折叠，传输中起关键作用 跨膜，并响应压力刺激。 HSC20是 在最近发现的 大肠杆菌中的操纵子也编码DNAK/HSP70型伴侣。 到 日期，尚未确定DNAJ辅助酮的结构。 我们 最近已经成功地过度夸张，净化和结晶 HSC20。 因此，HSC20可以提供第一个完整的高分辨率 该类别的蛋白质的晶体结构。