The authors concluded that for the hTLR1-TLR2 complex, three residues -Q97, N99, Y136 of TLR1, and two residues -E55, K62 of TLR2 impact the binding energy of the complex. For the hTLR2-TLR6 complex, the following residues were predicted to have a significant role: Y44, W45 of TLR2 and E159, K160 of TLR6. While combining the results of alanine scanning mutation studies with sequence alignment, structure prediction and superimposition, molecular docking, and MD simulations, the authors presented two key conclusions. The first was that the subtle conformational variations in the TLR structures might play a crucial role during special circumstances. The second was that the role of TLR2 BB-loop residues and TLR1/TLR6 near-DD-loop residues is important for the process of heterodimerisation and for initiating differential downstream signalling.