Title : The molecular structure of the
Toll-like receptor 3 ligand-binding
domain
Abstract :
- Innate immunity is the first line of defense against invading pathogens
- Toll-like receptors ( TLRs ) act as sentinels of the innate immune system, sensing a variety of ligands from lipopolysaccharide to flagellin to dsRNA through their ligand-binding domain that is composed of leucine-rich repeats (LRRs)
- Ligand binding initiates a signaling cascade that leads to the up-regulation of inflammation mediators
- In this study, we have expressed and crystallized the ectodomain ( ECD ) of human TLR3 , which recognizes dsRNA, a molecular signature of viruses, and have determined the molecular structure to 2.4-A resolution
- The overall horseshoe-shaped structure of the TLR3- ECD is formed by 23 repeating LRRs that are capped at each end by specialized non-LRR domains
- The extensive beta-sheet on the molecule's concave surface forms a platform for several modifications, including insertions in the LRRs and 11 N-linked glycans
- The TLR3- ECD structure indicates how LRR loops can establish distinct pathogen recognition receptors
Output (sent_index, trigger,
protein,
sugar,
site):
- 2. leucine-rich, , -, leucine-rich repeats, leucine
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):