STRUCTURAL AND FUNCTIONAL LIGAND-BINDING FEATURES OF USP

USP 的结构和功能配体结合特征

• 批准号: 6387028
• 负责人: GRACE M JONES
• 金额: $ 25.65万
• 依托单位: UNIVERSITY OF KENTUCKY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-05-01 至 2003-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6387028
• 关键词: Drosophilidae; alkyltransferase; conformation; ecdysone; gel mobility shift assay; gene mutation; human tissue; juvenile hormones; ligands; point mutation; protein binding; protein protein interaction; protein structure function; steroid hormone receptor; transcription factor; yeast two hybrid system

DESCRIPTION (Adapted from the Applicant's Abstract): The long term objective of this research is to determine the mechanisms by which the invertebrate nuclear receptor, ultraspiracle, transduces the regulatory signals of its endogenous ligands(s) into pathways for transcriptional activation. The proposed research builds upon their recent studies that have demonstrated that two natural dipteran epoxymethylfarnesoates bind with specificity to ultraspiracle so as to cause conformational change in that receptor, while closely related farnesoid pathway metabolites do not have this interaction with USP.

描述（改编自申请人的摘要）： 这项研究是为了确定无脊椎动物的核 受体，ultraspiracle，转导其内源性的调节信号， 配体进入转录激活的途径。拟议研究 他们最近的研究表明， 双翅目环氧甲基法呢酸酯特异性结合超气门， 引起受体构象变化，而与法尼醇密切相关 途径代谢物与USP没有这种相互作用。