Structural analysis of toll-like receptors

Jungwoo Choe, Ian A. Wilson

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review


Toll-like receptors (TLRs) represent a primary line of defense against invading pathogens, including bacteria, viruses, fungi, and parasites.1,2 Recognition of conserved microbial components by these receptors triggers innate immune responses that result in inflammation, antiviral responses, and maturation of dendritic cells, and ultimately leads to the clearance of the infectious agents. TLRs contain extracellular domains with leucine-rich repeats for ligand binding and intracellular Toll/interleukin- 1 receptor (TIR) domains for signaling. The ligand binding domain of a TLR recognizes various pathogen-associated molecules, including lipopeptide (ligand of TLR2), double-stranded RNA (TLR3), lipopolysaccharide (TLR4), flagellin (TLR5), single-stranded RNA (TLR7), and unmethylated CpG DNA (TLR9).3,4 The intracellular TIR domain interacts with TIR domains in adaptor molecules such as MyD88, TIRAP, TRIF, and TRAM to initiate pathogen-specific immune responses,5,6.

Original languageEnglish
Title of host publicationNucleic Acids in Innate Immunity
PublisherCRC Press
Number of pages14
ISBN (Electronic)9781420068269
ISBN (Print)9781420068252
StatePublished - 1 Jan 2008


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