STRUCTURAL STUDIES OF FF DOMAINS

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。 FF域是最近发现的一个蛋白质-蛋白质相互作用模块。它长约50个残基，含有两个保守的苯丙氨酸残基(Ff)。Ff结构域存在于多种真核蛋白质中，包括前mRNA剪接因子Prp40、转录延伸因子CA150、Forin结合蛋白11和p190RhoGAP。FF域通常以排列的方式以串联拷贝的形式出现，并且经常伴随WW域。到目前为止，Ff结构域除了与RNA聚合酶II的过度磷酸化的C末端重复结构域相互作用外，还没有太多的生物学功能。结构研究也很有限。单一的FF域只有两种核磁共振结构。我们已经结晶了一个含有三个FF结构域的结构，并收集了一些来自ALS的初步衍射。新的数据收集将导致确定新的结构，这将阐明金融框架领域的安排及其所涉功能问题。

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. FF domain is a recently discovered protein-protein interaction module. It is ~50 residues in length bearing two conserved phenylalanine residues (FF). FF domain is found in a variety of eukaryotic proteins including pre-mRNA splicing factor Prp40, transcription elongation factor CA150, formin-binding protein 11 and p190RhoGAP. The FF domain often occurs as tandem copies in an arrayed manner and often accompanies WW domains. So far not much biological function has been assigned to the FF domain except that it can interact with the hyperphosphorylated C-terminal repeat domain (phospho-CTD) of RNA polymerase II. Structural studies have also be limited. There are only two NMR structures of single FF domains. We have crystallized a construct containing three FF domains and have collected some preliminary diffraction from ALS. New data collection will lead to determination of a new structure which will shed light on the arrangement of the FF domains and their functional implications.