Conserved water mediated H-bonding dynamics of Ser117 and Thr119 residues in human transthyretin-thyroxin complexation: Inhibitor modeling study through docking and molecular dynamics simulation

Article ID	Journal	Published Year	Pages	File Type
6877756	Journal of Molecular Graphics and Modelling	2013	11 Pages	PDF

Abstract

- One water molecule bridging Ser117 and Thr119 of transthyretin is conserved in X-ray and MD simulated structures.
- This conserved hydrophilic center plays a salient role in T4 (thyroxin)-TTR complexation.
- MD simulation and docking studies have been used for inhibitor design.
- Four thyroxin modified inhibitors have been designed using conserved water mimic inhibitor design protocol.
- Theoretical studies indicate the plausibility of Mod4 to act as better inhibitor.

Keywords

MOD halogen binding pocket familial amyloid cardiomyopathy total polar surface area tPSA HBP RBP FAP SSA HTTR FAC Familial amyloidotic polyneuropathy Amyloid senile systemic amyloidosis modified Thyroxin Docking Molecular dynamics Molecular dynamics simulation CSF Cerebrospinal fluid Retinol-binding protein Kelvin