The authors performed MD simulations together with PCA, RIN, hydrogen bond and proteinnucleic acid interaction analyses to investigate the global motions and the distribution of crucial residues for signal transduction. They claimed that apo wild-type pre-formed dimer is unlikely to be stable in physiological conditions. Thus, they proposed that TLR3 might exist as a monomer in a solution. Further, the interaction energies and hydrogen bonds analyses indicated that the mutations induced certain conformational changes which could disturb the TLR3 signalling. The interaction sites between TLR3 and dsRNA were observed at both the N-terminal and C-terminal ends of TLR3 LRR, while the dimerisation interface was confirmed at the C-terminal site but only for dTLR3WT-dsRNA and dTLR3L412F-dsRNA. It might suggest that P680 is crucial for maintaining the dimer interface for ligand binding.