Crystallographic Study of Novel Transthyretin Ligands Exhibiting Negative-Cooperativity between Two Thyroxine Binding Sites.
Tomar, D., Khan, T., Singh, R.R., Mishra, S., Gupta, S., Surolia, A., Salunke, D.M.(2012) PLoS One 7: 43522
- PubMed: 22973437 
- DOI: https://doi.org/10.1371/journal.pone.0043522
- Primary Citation of Related Structures:  
4ABQ, 4ABU, 4ABV, 4ABW, 4AC2, 4AC4, 4ANK - PubMed Abstract: 
Transthyretin (TTR) is a homotetrameric serum and cerebrospinal fluid protein that transports thyroxine (T4) and retinol by binding to retinol binding protein. Rate-limiting tetramer dissociation and rapid monomer misfolding and disassembly of TTR lead to amyloid fibril formation in different tissues causing various amyloid diseases. Based on the current understanding of the pathogenesis of TTR amyloidosis, it is considered that the inhibition of amyloid fibril formation by stabilization of TTR in native tetrameric form is a viable approach for the treatment of TTR amyloidosis.
Organizational Affiliation: 
Structural Biology Unit, National Institute of Immunology, New Delhi, India.