Figure 5
From: The Architecture of the TIR Domain Signalosome in the Toll-like Receptor-4 Signaling Pathway
Possible TIR domain signalosome models for FF TLR4-dimer.
(a) Interaction model of monomeric-MyD88 with TLR4 and Mal dimers. (b,c) MyD88-dependent TIR-domain signalosome models for FF TLR4-dimer. All proteins are in dimer form, including TLR4, Mal and MyD88. It is known that dimeric MyD88 has higher affinity to stimulated TLRs due to their extended interfaces. In line with this, models (b,c) show that the second MyD88 of the MyD88-dimer is very close to TLR4. Especially in part-c, one of the MyD88 molecules in the dimer is bound to Mal and the other is bound to TLR4. We obtained these complexes by superimposition of the binary interaction models of TLR4-TLR4, TLR4-Mal, Mal-Mal, Mal-MyD88 and MyD88-MyD88.
