STRUCTURAL STUDIES OF FF DOMAINS

FF 域的结构研究

• 批准号: 7722010
• 负责人: XIAOMIN CHEN
• 金额: $ 0.02万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2008
• 资助国家: 美国
• 起止时间: 2008-03-01 至 2009-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7722010
• 关键词: Amyotrophic Lateral Sclerosis; Binding Proteins; Biological Process; C-terminal; Computer Retrieval of Information on Scientific Projects Database; Data Collection; Funding; Grant; Heterogeneous Nuclear RNA; Institution; Lead; Length; Light; Phenylalanine; Proteins; RNA Polymerase II; RNA Splicing; Research; Research Personnel; Resources; Source; Structure; Terminal Repeat Sequences; Transcription Elongation; United States National Institutes of Health; mRNA Precursor; protein protein interaction

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.

这个子项目是许多利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。列出的机构为 中心，但不一定是研究者所在的机构。 FF结构域是近年来发现的蛋白质相互作用模块。它的长度约为50个残基，带有两个保守的苯丙氨酸残基（FF）。FF结构域存在于多种真核生物蛋白中，包括前mRNA剪接因子Prp 40、转录延伸因子CA 150、formin结合蛋白11和p190 RhoGAP。FF结构域通常以阵列方式作为串联拷贝出现，并且通常伴随WW结构域。到目前为止，除了FF结构域可以与RNA聚合酶II的高度磷酸化的C-末端重复结构域（磷酸-CTD）相互作用外，还没有太多的生物学功能被分配给FF结构域。结构研究也很有限。单个FF结构域只有两种NMR结构。我们已经结晶了一个含有三个FF域的结构，并收集了一些初步的ALS衍射。新的数据收集将导致确定一个新的结构，这将阐明FF域的安排及其功能的影响。