STRUCTURAL STUDIES OF FF DOMAINS

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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.