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Ligand recognition by the toll?like receptor family

Animal Cells and Systems 2009년 13권 1호 p.1 ~ 8
진미선, 이지오,
소속 상세정보
진미선 ( Jin Mi-Sun ) - Korea Advanced Institute of Science and Technology Department of Nanoscience and Technoloogy
이지오 ( Lee Jie-Oh ) - Korea Advanced Institute of Science and Technology Department of Chemistry

Abstract


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.

키워드

innate immune response; leucine rich repeat; pattern recognition receptor; toll?like receptor; hybrid LRR technique

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