STRUCTURAL STUDIES OF NATIVE AND DESIGNED ALPHA HELICAL COILED COILS

原生和设计的 α 螺旋线圈的结构研究

• 批准号: 8169243
• 负责人: AMY E KEATING
• 金额: $ 0.09万
• 依托单位: CORNELL UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-04-01 至 2011-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169243
• 关键词: Coiled-Coil Domain; Computer Analysis; Computer Retrieval of Information on Scientific Projects Database; Funding; Genetic Transcription; Grant; Human; Institution; Measurement; Modeling; Peptides; Proteins; Proteome; Research; Research Personnel; Resources; Source; Specificity; Structure; United States National Institutes of Health; Yeasts; combinatorial; design; dimer; interest; programs; spindle pole body; transcription factor

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. Research in the Keating lab aims to understand determinants of structural specificity and interaction specificity in alpha-helical coiled coils, a common interaction motif in the proteome. We apply an integrated program of experimental measurement, computational analysis, and structure determinantion. Targets of particular interest include bZIP transcription factors and coiled coils of the yeast spindle pole body. For the bZIPs, combinatorial interactions that regulate transcription are made via coiled-coil dimers. We are studying both native and synthetic coiled-coil peptides that interact with human bZIPs by forming coiled-coil dimers. Proteins of the spindle pole body are highly enriched in predicted coiled-coil domains, and we are characterizing these as part of an effort to build models of the overall structure of the very large spindle pole body assembly.

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表示。列出的机构是 对于中心，这不一定是调查员的机构。 Keating Lab中的研究旨在了解α-螺旋线圈中结构特异性和相互作用特异性的决定因素，这是蛋白质组中常见的相互作用基序。我们应用了实验测量，计算分析和结构决定性的集成程序。特别感兴趣的靶标包括BZIP转录因子和酵母纺锤体体的盘绕线圈。对于BZIPS，调节转录的组合相互作用是通过盘绕螺旋二聚体进行的。我们正在研究通过形成盘绕螺旋二聚体与人BZIP相互作用的天然和合成螺旋线圈肽。主轴杆体的蛋白质高度富含预测的盘绕螺旋域，我们将其表征为构建非常大的纺锤体体形组件的整体结构模型的一部分。