STRUCTURAL STUDIES OF NATIVE AND DESIGNED ALPHA HELICAL COILED COILS

该子项目是利用资源的许多研究子项目之一 由NIH/NCRR资助的中心赠款提供。次级项目的主要支助 子项目的主要研究者可能是由其他来源提供的， 包括其他NIH来源。 为子项目列出的总成本可能 表示子项目使用的中心基础设施的估计数量， NCRR赠款不直接向子项目或子项目工作人员提供资金。 Keating实验室的研究旨在了解α-螺旋卷曲螺旋中结构特异性和相互作用特异性的决定因素，α-螺旋卷曲螺旋是蛋白质组中常见的相互作用基序。我们采用实验测量、计算分析和结构测定的综合方案。特别感兴趣的靶标包括bZIP转录因子和酵母纺锤体极体的卷曲螺旋。对于bZIPs，调节转录的组合相互作用通过卷曲螺旋二聚体进行。我们正在研究天然和合成的卷曲螺旋肽，通过形成卷曲螺旋二聚体与人bZIPs相互作用。蛋白质的纺锤体极体高度富集在预测的卷曲螺旋结构域，我们正在表征这些作为一项努力的一部分，以建立模型的整体结构非常大的纺锤体极体大会。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.