DETERMINING THE ARCHITECTURES OF MACROMOLECULAR ASSEMBLIES

确定大分子组装体的结构

• 批准号: 7722246
• 负责人: MICHAEL P ROUT
• 金额: $ 2.22万
• 依托单位: ROCKEFELLER UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7722246
• 关键词: Architecture; Biological Models; Cell Nucleus; Cells; Collection; Computer Retrieval of Information on Scientific Projects Database; Data; Data Quality; Evolution; Funding; Grant; Institution; Life; Maps; Nuclear Pore Complex; Paper; Process; Proteins; Proteomics; Research; Research Personnel; Resources; Source; Structure; Translations; United States National Institutes of Health; Work; Yeasts; insight; macromolecular assembly; restraint

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. To understand the workings of a living cell, we need to know the architectures of its macromolecular assemblies. Here we show how proteomic data can be used to determine such structures. The process involves the collection of sufficient and diverse high-quality data, translation of these data into spatial restraints, and an optimization that uses the restraints to generate an ensemble of structures consistent with the data. Analysis of the ensemble produces a detailed architectural map of the assembly. We developed our approach on a challenging model system, the nuclear pore complex (NPC). The NPC acts as a dynamic barrier, controlling access to and from the nucleus, and in yeast is a 50 MDa assembly of 456 proteins. The resulting structure, presented in an accompanying paper, reveals the configuration of the proteins in the NPC, providing insights into its evolution and architectural principles. The present approach should be applicable to many other macromolecular assemblies.

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