Reconstructing the TIR Side of the Myddosome: a Paradigm for TIR-TIR Interactions.

@article{Vyncke2016ReconstructingTT,
  title={Reconstructing the TIR Side of the Myddosome: a Paradigm for TIR-TIR Interactions.},
  author={Laurens Vyncke and Celia Bovijn and Ewald Pauwels and Tim Van Acker and Elien Ruyssinck and Elianne Burg and Jan Tavernier and Frank Peelman},
  journal={Structure},
  year={2016},
  volume={24 3},
  pages={437-47}
}
Members of the Toll-like receptor and interleukin-1 (IL-1) receptor families all signal via Toll/IL-1R (TIR) domain-driven assemblies with adaptors such as MyD88. We here combine the mammalian two-hybrid system MAPPIT and saturation mutagenesis to complement and extend crystallographic and nuclear magnetic resonance data, and reveal how TIR domains interact. We fully delineate the interaction sites on the MyD88 TIR domain for homo-oligomerization and for interaction with Mal and TLR4… CONTINUE READING
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Crystal structure of TIR domain of TLR6 reveals novel dimeric interface of TIR-TIR interaction for Toll-like receptor signaling pathway

Jang, T.-H, H. H. Park
J. Mol. Biol • 2014

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