STRUCTURAL STUDIES OF NATIVE AND DESIGNED ALPHA HELICAL COILED COILS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 基廷实验室的研究旨在了解阿尔法螺旋螺旋线圈的结构特异性和相互作用特异性的决定因素，阿尔法螺旋螺旋线圈是蛋白质组中常见的相互作用基序。我们应用了一个集实验测量、计算分析和结构确定于一体的程序。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线圈。对于bZIP，调节转录的组合相互作用是通过盘绕线圈二聚体进行的。我们正在研究天然和合成的盘绕多肽，它们通过形成盘绕二聚体与人的bZIP相互作用。纺锤极体的蛋白质在预测的螺旋线圈结构域中高度丰富，我们正在对这些蛋白质进行表征，作为建立超大型纺锤杆体组件整体结构模型的一部分。

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.