Structural insight to mutated Y116S transthyretin by molecular dynamics simulation

Avik Banerjee, Hridoy R. Bairagya, Bishnu P. Mukhopadhyay, Tapas K. Nandi, Asim K. Bera

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


Familial amyloidotic polyneuropathy (FAP) is strictly associated with point mutations of transthyretin (TTR) protein. The Tyr1 16→Ser (Y116S) mutant TTR is an important amyloidogenic variant responsible for FAP. Structural dynamics of monomeric TTR and its mutant (Y116S) may give some clue relating to amyloid formation. In this study, molecular dynamic simulation at 310 K has been performed on wild-type and mutant (Y116S) TTR monomer, which can provide the molecular insight of structural transition in the inner and outer strand of the protein. Results show that mutation in the H-strand (Tyr116→Ser) leads to disruption of secondary structure and H-bonding pattern of some important parts of the inner DAGH-sheet of the protein. Especially, the residues T106, A108, L1 10 of G-strand, S1 17 and T119 of H-strand are affected, which are involved in the binding of thyroxin hormone. This unfolding of mutant structure during dynamics may cause instability in the protein and thus induce amyloidgenesis.

Original languageEnglish (US)
Pages (from-to)197-202
Number of pages6
JournalIndian Journal of Biochemistry and Biophysics
Issue number4
StatePublished - Aug 2010


  • Amyloid
  • Fibrils
  • Human transthyretin
  • Molecular dynamics simulation


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