Microcrystal electron diffraction structure of Toll-like receptor 2 TIR-domain-nucleated MyD88 TIR-domain higher-order assembly.

ABSTRACT: Eukaryotic TIR (Toll/interleukin-1 receptor protein) domains signal via TIR-TIR interactions, either by self-association or by interaction with other TIR domains. In mammals, TIR domains are found in Toll-like receptors (TLRs) and cytoplasmic adaptor proteins involved in pro-inflammatory signaling. Previous work revealed that the MAL TIR domain (MAL^TIR) nucleates the assembly of MyD88^TIR into crystalline arrays in vitro. A microcrystal electron diffraction (MicroED) structure of the MyD88^TIR assembly has previously been solved, revealing a two-stranded higher-order assembly of TIR domains. In this work, it is demonstrated that the TIR domain of TLR2, which is reported to signal as a heterodimer with either TLR1 or TLR6, induces the formation of crystalline

SUBMITTER: Li Y 

PROVIDER: S-EPMC11394124 | biostudies-literature | 2024 Sep

REPOSITORIES: biostudies-literature