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.

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