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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The dsRNA binding site of human Toll-like receptor 3
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The dsRNA binding site of human Toll-like receptor 3

机译：人类Toll样受体3的dsRNA结合位点

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摘要

Pathogen recognition by Toll-like receptors (TLRs) initiates innate immune responses that are essential for inhibiting pathogen dissemination and for the development of acquired immunity. The TLRs recognize pathogens with their N-terminal ectodomains (ECD), but the molecular basis for this recognition is not known. Recently we reported the x-ray structure for unliganded TLR3-ECD; however, it has proven difficult to obtain a crystal structure of TLR3 with its ligand, dsRNA. We have now located the TLR3 ligand binding site by mutational analysis. More than 50 single-residue mutations have been generated throughout the TLR3-ECD, but only two, H539E and N541A, resulted in the loss of TLR3 activation and ligand binding functions. These mutations locate the dsRNA binding site on the glycan-free, lateral surface of TLR3 toward the C terminus and suggest a model for dsRNA binding and TLR3 activation.
机译：Toll样受体（TLR）识别病原体会引发先天性免疫反应，这对于抑制病原体传播和获得性免疫的发展至关重要。 TLR识别具有其N末端胞外域（ECD）的病原体，但是这种识别的分子基础尚不清楚。最近，我们报道了未配体的TLR3-ECD的X射线结构。然而，已证明难以获得具有其配体dsRNA的TLR3的晶体结构。我们现在通过突变分析确定了TLR3配体结合位点。在整个TLR3-ECD中已经产生了50多个单残基突变，但是只有两个H539E和N541A导致TLR3活化和配体结合功能丧失。这些突变将dsRNA结合位点定位在TLR3的无糖侧面上朝向C末端，并提示了dsRNA结合和TLR3激活的模型。

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