TLR3 forms a laterally aligned multimeric complex along double-stranded RNA for efficient signal transduction.

ABSTRACT: Toll-like receptor 3 (TLR3) is a member of the TLR family, which plays an important role in the innate immune system and is responsible for recognizing viral double-stranded RNA (dsRNA). Previous biochemical and structural studies have revealed that a minimum length of approximately 40-50 base pairs of dsRNA is necessary for TLR3 binding and dimerization. However, efficient TLR3 activation requires longer dsRNA and the molecular mechanism underlying its dsRNA length-dependent activation remains unknown. Here, we report cryo-electron microscopy analyses of TLR3 complexed with longer dsRNA. TLR3 dimers laterally form a higher multimeric complex along dsRNA, providing the basis for cooperative binding and efficient signal transduction.

SUBMITTER: Sakaniwa K 

PROVIDER: S-EPMC9834221 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature