STRUCTURE OF COMPLEX BETWEEN TFIIIA & ITS 31 BP DNA SITE

TFIIIA 之间的复合体结构

• 批准号: 6437543
• 负责人: STEPHEN COPLAN HARRISON
• 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/6437543
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; genome; proteins; radiography; structural biology

Multiple zinc finger motifs were originally discovered in Xenopus transcription factor IIIA (TFIIIA). Each motif is an independently folded protein domain. Nine tandem zinc fingers are present in TFIIIA, allowing the protein to bind to an extensive region of the 5S RNA gene promoter. There is a relatively "standard" docking of most of the fingers represented in set into the major groove of DNA, but the GLI structure shows one finger with essentially no DNA contacts. Thus, proteins with more than 3 fingers may have highly divergent docking modes. The goal of the present study is to examine a still longer complex.

最初在非洲爪蟾身上发现了多个锌指图案