Ligand Recognition by the Toll-like Receptor Family

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Toll-like receptor (TLR) family proteins, type I transmembrane proteins, play a central role in human innate immune response by recognizing common structural patterns in diverse molecules from bacteria, viruses and fungi. Recently four structures of the TLR and ligand complexes have been determined by high resolution x-ray crystallographic technique. In this review we summarize reported structures of TLRs and their proposed activation mechanisms. The structures demonstrate that binding of agonistic ligands to the extracellular domains of TLRs induces homo- or heterodimerization of the receptors. Dimerization of the TLR extracellular domains brings their two C-termini into close proximity. This suggests a plausible mechanism of TLR activation: ligand induces dimerization of the extracellular domains, which enforces juxtaposition of intracellular signaling domains for recruitment of intracellular adaptor proteins for signal initiation.
Publisher
ZOOLOGICAL SOC KOREA
Issue Date
2009-03
Language
English
Article Type
Review
Keywords

LEUCINE-RICH REPEATS; LIPOTEICHOIC ACID LTA; DOUBLE-STRANDED-RNA; CRYSTAL-STRUCTURE; STREPTOCOCCUS-PNEUMONIAE; STAPHYLOCOCCUS-AUREUS; ENDOTOXIN ANTAGONIST; STRUCTURAL DIVERSITY; CYTOKINE INDUCTION; IMMUNE-RESPONSE

Citation

ANIMAL CELLS AND SYSTEMS, v.13, no.1, pp.1 - 8

ISSN
1976-8354
URI
http://hdl.handle.net/10203/94235
Appears in Collection
CH-Journal Papers(저널논문)
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