ABSTRACT
The systemic deposition of transthyretin (TTR) under the form of insoluble fibrils is the hallmark of TTR amyloid related diseases. Senile Systemic Amyloidosis is characterized by the presence of protein deposits containing the wild-type (WT) protein, whereas a point mutation in the amino acid sequence is the biochemical marker for Familial Amyloidotic Polyneuropathy. The chapter analyses the three dimensional structure of the TTR Tyr78Phe variant. Crystals of the recombinant TTR Tyr78Phe were grown by vapour diffusion methods. As it has been reported for most TTR variants, the final refined model obtained for TTR Tyr78Phe displays a high overall homology to the structure of the WT-protein deposited in the PDB.
