The reviewed papers revealed important insight into TLRs dynamics. In summarised studies, authors presented relevant information on possible changes in position and conformation that receptors embedded in the cell membrane or intracellular compartments may undergo. Also, an important message regarding the potential mechanism of TIR domain dimerisation and binding of the adaptor protein came from the analysed models of both symmetrical and asymmetrical domains. This may be helpful for designing new types of TLR modulators, especially those targeting the TIR domain. One should remember that the presented studies referred only to TLR3 and TLR4, which means that for now, the conclusions can not be unified for all other receptors.