期刊
IMMUNITY
卷 29, 期 2, 页码 182-191出版社
CELL PRESS
DOI: 10.1016/j.immuni.2008.07.007
关键词
-
类别
资金
- Ministry of Education, Science and Technology
- Korean Science and Engineering Foundation
- Ministry of Education, Science & Technology (MoST), Republic of Korea [Kaist_KI_2008_69] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
- National Research Foundation of Korea [R16-2008-007-01001-0, 과06A1506] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Toll-like receptors (TLRs) play central roles in the innate immune response by recognizing conserved structural patterns in diverse microbial molecules. Here, we discuss ligand binding and activation mechanisms of the TLR family. Hydrophobic ligands of TLR1, TLR2, and TLR4 interact with internal protein pockets. In contrast, dsRNA, a hydrophilic ligand, interacts with the solvent-exposed surface of TLR3. Binding of agonistic ligands, lipopeptides or dsRNA, induces dimerization of the ectodomains of the various TLRs, forming dimers that are strikingly similar in shape. In these m-shaped complexes, the C termini of the extracellular domains of the TLRs converge in the middle. This observation suggests the hypothesis that dimerization of the extracellular domains forces the intracellular TIR domains to dimerize, and this initiates signaling by recruiting intracellular adaptor proteins.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据