The Structural Biology of Toll-Like Receptors
By I. Botos, D. Segal, D. Davies. Structure, 2011
637 citations recorded by the source corpus.
The membrane-bound Toll-like receptors (TLRs) trigger innate immune responses following recognition of a wide variety of pathogen-derived compounds. Despite the wide range of ligands recognized by TLRs, the receptors share a common structural framework in their extracellular, ligand-binding domains. These domains all adopt horseshoe-shaped structures built from leucine-rich repeat motifs. Typically, upon ligand binding, two extracellular domains form an “m”-shaped dimer sandwiching the ligand molecule bringing the transmembrane and cytoplasmic domains in close proximity and triggering a downstream signalling cascade. Although the ligand-induced dimerization of these receptors has many common features, the nature of the interactions of the TLR extracellular domains with their ligands varies markedly between TLR paralogs.
Subfields: Biochemistry, Immunology, Pharmacology
View Paper: https://www.semanticscholar.org/paper/7d83b8cfc7fc7d1d9914fb633100e584e846d362
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In Immunology
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Citations in the corpus
- Mitochondrial dysfunction: mechanisms and advances in therapy (2024, background): “163 TLRs are synthesized within the ER, proceeding through the Golgi apparatus before their distribution to intracellular loci, where they are poised to recognize unmethylated CpG-DNA motifs, notably including mtDNA.”
- Pattern recognition receptors in health and diseases (2021, background): “1).(49,77,78) Lee revealed that TLR10 binds dsRNA in vitro at endosomal pH, indicating that dsRNA is a ligand of TLR10.”
- Toll-Like Receptor Signaling Pathways (2014, background): “The lipid-binding domain of TIRAP binds to PI(4,5)P2 at the plasma membrane and to PI(3)P on endosomes, which mediates the formation of functional TLR4 and TLR9 signaling complexes at their respective sites.”