- EMDB-32599: Cryo-EM structure of tetrameric TLR3 in complex with dsRNA (90 bp) -
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基本情報
登録情報
データベース: EMDB / ID: EMD-32599
タイトル
Cryo-EM structure of tetrameric TLR3 in complex with dsRNA (90 bp)
マップデータ
試料
複合体: Tetrameric TLR3 in complex with dsRNA (90 bp)
タンパク質・ペプチド: Toll-like receptor 3
RNA: RNA (81-MER)
RNA: RNA (81-MER)
リガンド: 2-acetamido-2-deoxy-beta-D-glucopyranose
キーワード
innate immunity / IMMUNE SYSTEM / IMMUNE SYSTEM-RNA complex
機能・相同性
機能・相同性情報
type III interferon production / positive regulation of type III interferon production / regulation of dendritic cell cytokine production / inflammatory response to wounding / toll-like receptor 3 signaling pathway / necroptotic signaling pathway / positive regulation of cytokine production involved in inflammatory response / positive regulation of macrophage cytokine production / toll-like receptor signaling pathway / pattern recognition receptor activity ...type III interferon production / positive regulation of type III interferon production / regulation of dendritic cell cytokine production / inflammatory response to wounding / toll-like receptor 3 signaling pathway / necroptotic signaling pathway / positive regulation of cytokine production involved in inflammatory response / positive regulation of macrophage cytokine production / toll-like receptor signaling pathway / pattern recognition receptor activity / cellular response to exogenous dsRNA / response to exogenous dsRNA / ubiquitin-like protein ligase binding / positive regulation of interferon-alpha production / positive regulation of type I interferon production / cellular response to interferon-beta / positive regulation of chemokine production / extrinsic apoptotic signaling pathway / JNK cascade / positive regulation of interleukin-12 production / positive regulation of interferon-beta production / positive regulation of interleukin-8 production / positive regulation of JNK cascade / microglial cell activation / positive regulation of non-canonical NF-kappaB signal transduction / defense response / cellular response to virus / cellular response to type II interferon / positive regulation of interleukin-6 production / response to virus / cellular response to mechanical stimulus / positive regulation of type II interferon production / male gonad development / positive regulation of angiogenesis / positive regulation of tumor necrosis factor production / cellular response to xenobiotic stimulus / transmembrane signaling receptor activity / MAPK cascade / double-stranded RNA binding / defense response to virus / early endosome / positive regulation of canonical NF-kappaB signal transduction / endosome membrane / positive regulation of apoptotic process / innate immune response / endoplasmic reticulum membrane / cell surface / positive regulation of transcription by RNA polymerase II / identical protein binding / plasma membrane 類似検索 - 分子機能
Ministry of Education, Culture, Sports, Science and Technology (Japan)
19J21830
日本
Ministry of Education, Culture, Sports, Science and Technology (Japan)
19H03164
日本
Ministry of Education, Culture, Sports, Science and Technology (Japan)
19H00976
日本
引用
ジャーナル: Nat Commun / 年: 2023 タイトル: TLR3 forms a laterally aligned multimeric complex along double-stranded RNA for efficient signal transduction. 著者: Kentaro Sakaniwa / Akiko Fujimura / Takuma Shibata / Hideki Shigematsu / Toru Ekimoto / Masaki Yamamoto / Mitsunori Ikeguchi / Kensuke Miyake / Umeharu Ohto / Toshiyuki Shimizu / 要旨: Toll-like receptor 3 (TLR3) is a member of the TLR family, which plays an important role in the innate immune system and is responsible for recognizing viral double-stranded RNA (dsRNA). Previous ...Toll-like receptor 3 (TLR3) is a member of the TLR family, which plays an important role in the innate immune system and is responsible for recognizing viral double-stranded RNA (dsRNA). Previous biochemical and structural studies have revealed that a minimum length of approximately 40-50 base pairs of dsRNA is necessary for TLR3 binding and dimerization. However, efficient TLR3 activation requires longer dsRNA and the molecular mechanism underlying its dsRNA length-dependent activation remains unknown. Here, we report cryo-electron microscopy analyses of TLR3 complexed with longer dsRNA. TLR3 dimers laterally form a higher multimeric complex along dsRNA, providing the basis for cooperative binding and efficient signal transduction.