It is now known that IDPs play significant roles in various biological events. IDPs, which are more usually found in the eukaryotic nucleus than the cytoplasm, are defined as proteins that fold and function upon target recognition. Our research group aims at identifying the common structural features of the target recognition mechanism of IDPs in the eukaryotic nucleus. Conventional structural biology characterizes the static structures of proteins with or without any target protein or DNA. In contrast, our research group is attempting to characterize dynamic structures for each state of the IDPs, the target-free state, the initial complex, folding intermediates, and the final bound complex. As a result, we intend to understand the shared elements of the molecular recognition mechanisms of IDPs from a structural viewpoint.
Our research targets are nuclear proteins, such as general transcription factors, transcription factors, splicing factors, and histone proteins. Dynamic structures of IDPs are characterized by NMR whereas structural changes of IDPs upon target binding are analyzed by mass spectrometry (MS). Moreover, we also develop the methodology for the dynamic structural analysis of IDPs by NMR and MS.