STRUCTURE-FUNCTION STUDIES ON C-TERMINAL TRUNCATIONS OF 11BHYDROXYSTERIOD DEHYDR

11B羟基甾碘脱水剂C端截断的结构与功能研究

• 批准号: 8170214
• 负责人: GYORGY SNELL
• 金额: $ 0.07万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170214
• 关键词: 11-beta-Hydroxysteroid Dehydrogenase Type 1; Adipose tissue; Computer Retrieval of Information on Scientific Projects Database; Cortisone; Crystallography; Disease; Drug Delivery Systems; Enzymes; Extracellular Structure; Funding; Grant; Human; Hydrocortisone; Institution; Membrane Proteins; Non-Insulin-Dependent Diabetes Mellitus; Obesity; Oxidoreductase; Pathogenesis; Production; Research; Research Personnel; Resolution; Resources; Source; Structure; United States National Institutes of Health

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Human 11beta-hydroxysteroid dehydrogenase type 1 (11beta-HSD1) is an ER-localized membrane protein that catalyzes the interconversion of cortisone and cortisol. In adipose tissue, excessive cortisol production through 11beta-HSD1 activity has been implicated in the pathogenesis of type II diabetes and obesity, which makes this enzyme a potential drug target against these diseases. Recently we have solved the first high-resolution crystal structure of the extracellular portion of the enzyme. We wish to undertake further studies on 11beta-HSD1 with regards to enzyme oligomerization and reductase activity. To this end, we would like to carry out systematic truncations of the C-terminus and use x-ray crystallography to understand the structural features controlling these two interrelated functions.

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