STRUCTURAL STUDIES OF NATURAL AND ENGINEERED ALLOSTERIC PROTEINS

天然和工程变构蛋白的结构研究

• 批准号: 8170098
• 负责人: Martin Sagermann
• 金额: $ 0.13万
• 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/8170098
• 关键词: Binding; Biocompatible Materials; Computer Retrieval of Information on Scientific Projects Database; Engineering; Funding; Grant; Institution; Laboratories; Methodology; Point Mutation; Procedures; Process; Proteins; Research; Research Personnel; Resources; Source; United States National Institutes of Health; combinatorial; design; functional restoration; improved

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. The artificial engineering of effector-induced conformational changes into proteins and biomaterials is envisioned to allow for the precise control of catalytic processes via external effectors. The structural mechanisms that permit allosteric changes in proteins, however, are only poorly understood. Research in our laboratory focuses on the design of allosteric proteins through a combination of combinatorial- and rational design procedures. Using new methodology developed in our laboratory we introduce destabilizing point mutations into selected target proteins. Specifically stabilizing interactions are engineered subsequently to restore function specifically under permissible conditions through the binding of specific effector molecules. Detailed structural characterizations are required to advance understanding of allosteric switches in general, and to optimize and improve the developed methodology.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 设想了效应诱导的构象变化对蛋白质和生物材料的人工工程，以通过外部效应子来精确控制催化过程。然而，允许蛋白质变构变化的结构机制仅了解蛋白质。我们实验室的研究重点是组合和理性设计程序的组合，介绍了变构蛋白的设计。使用在实验室中开发的新方法，我们将不稳定点突变引入选定的靶蛋白中。特异性稳定相互作用随后被设计为通过特定效应分子的结合在允许条件下特异性恢复功能。需要详细的结构特征来提高对变构开关的理解，并优化和改善开发的方法。