Backbone Nmr Chemical Shift Assignment Of Transthyretin

Transthyretin (TTR) is an important transporter protein for thyroxine (T-4) and a holoretinol protein in human. In its native state, TTR forms a tetrameric complex to construct the hydrophobic binding pocket for T-4. On the other hand, this protein is also infamous for its amyloidogenic propensity, which causes various human diseases, such as senile systemic amyloidosis and familial amyloid polyneuropathy/cardiomyopathy. In this work, to investigate various structural features of TTR with solution-state nuclear magnetic resonance (NMR) spectroscopy, we conducted backbone NMR signal assignments. Except the N-terminal two residues and prolines, backbone H-1-N-15 signals of all residues were successfully assigned with additional chemical shift information of (CO)-C-13, Ca-13(alpha), and C-13(beta) for most residues. The chemical shift information reported here will become an important basis for subsequent structural and functional studies of TTR.