Structure-Function Analysis of Alpha-Actinin Assembly

α-肌动蛋白组装的结构功能分析

• 批准号: 9304746
• 负责人: David Speicher
• 金额: $ 27万
• 依托单位: Wistar Institute
• 依托单位国家: 美国
• 项目类别: Continuing Grant
• 财政年份: 1993
• 资助国家: 美国
• 起止时间: 1993-08-01 至 1997-01-31
• 项目状态: 已结题
• 来源: https://www.nsf.gov/awardsearch/showAward?AWD_ID=9304746&HistoricalAwards=false
• 关键词: Structure; Function; Analysis; Alpha; Actinin

9304746 Speicher This proposal seeks to describe the mechanism by which alpha actinin forms homodimers. The approach is primarily biochemical, involving chemical cross-linking and site directed mutagenesis. %%% Alpha actinin is involved in the organization and function of muscle and is also involved in cell-to-cell and cell-to-substratum adhesion. Electron microscopic studies have resulted in low resolution models for alpha actinin structure, which involve alpha actinin dimers. The protein chemical studies proposed will establish at an atomic level whether the current model is correct and will further refine our understanding of the function of this important representative of a class of organizational biomolecules. ***

9304746 Speicher该建议试图描述α辅肌动蛋白形成同源二聚体的机制。 该方法主要是生物化学的，包括化学交联和定点诱变。 α辅肌动蛋白参与肌肉的组织和功能，也参与细胞与细胞和细胞与基质的粘附。 电子显微镜研究已经导致低分辨率模型的α辅肌动蛋白结构，其中涉及α辅肌动蛋白二聚体。 提出的蛋白质化学研究将在原子水平上确定目前的模型是否正确，并将进一步完善我们对一类组织生物分子的重要代表的功能的理解。 ***