ACTIVIN STRUCTURE-FUNCTION RELATIONSHIPS

激活素结构-功能关系

• 批准号: 6577253
• 负责人: WOLFGANG H FISCHER
• 金额: $ 19.74万
• 依托单位: SALK INSTITUTE FOR BIOLOGICAL STUDIES
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-04-01 至 2003-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6577253
• 关键词: X ray crystallography; biological signal transduction; cell line; chimeric proteins; follistatin; growth factor receptors; hormone binding protein; hormone receptor; inhibin; mutant; peptide hormone analog; point mutation; protein protein interaction; protein purification; protein structure function; receptor binding; recombinant proteins; site directed mutagenesis; transforming growth factors; X ray crystallography; biological signal transduction; cell line; chimeric proteins; follistatin; growth factor receptors; hormone binding protein; hormone receptor; inhibin; mutant; peptide hormone analog; point mutation; protein protein interaction; protein purification; protein structure function; receptor binding; recombinant proteins; site directed mutagenesis; transforming growth factors

Activin is a pluripotent hormone/growth factor that is involved in important biological functions including reproduction, development, and cell differentiation and survival. This Project studies the molecular events that lead to signal propagation by this protein. Activin interacts with two classes of cell surface mutant activin molecules to study the events that initiate signal transduction. We will employ X-ray crystallographic and mutagenesis data obtained by this Program to design these mutants. The initial interaction with activin type II receptors will be analyzed in detail. The mechanism of interaction with type I regulation of these events will be investigated. To further our understanding of the specific activities of the related proteins activin and TGFbeta, we will generate chimeric molecules and test these in biological systems specific for each of these factors.

激活素是一种多能激素/生长因子，参与重要的生物学功能，包括繁殖，发育和细胞分化和生存。该项目研究了导致该蛋白质信号传播的分子事件。激活素与两类的细胞表面突变激活素分子相互作用，以研究启动信号转导的事件。我们将采用该程序获得的X射线晶体学和诱变数据来设计这些突变体。将详细分析与II型受体的初始相互作用。将研究与这些事件I型调节的相互作用机制。为了进一步了解相关蛋白激活素和TGFBETA的特定活性，我们将生成嵌合分子，并在针对这些因素的特定生物系统中测试这些分子。