Parts, assembly and operation of the RIG-I family of motors.

Parts, assembly and operation of the RIG-I family of motors.
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DOI:
10.1016/j.sbi.2013.11.011
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发表时间:
2014-04
影响因子:
6.8
通讯作者:
Pyle AM
Pyle AM
中科院分区:
生物学2区
文献类型:
--
作者:
Rawling DC;Pyle AM

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宿主细胞入侵受到一系列模式识别受体(PRR)的监测,这些受体在检测到同源的病原体相关分子模式(PAMP)时会激活先天免疫机制。PRR中的RIG - I样受体(RLR)家族包括三种蛋白质——RIG - I、MDA5和LGP2——负责检测细胞内的致病性RNA。所有RLR蛋白质都围绕一个与典型的第2超家族(SF2)RNA解旋酶中发现的ATP酶核心同源的结构构建,该核心通过添加新的辅助结构域以识别双链RNA而被改造。本综述重点关注RLR中病原体特异性双链RNA结合和ATP酶激活的结构基础、RLR家族成员对RNA的差异识别,以及对其他双链RNA激活的ATP酶(如Dicer)的影响。
Host cell invasion is monitored by a series of pattern recognition receptors (PRRs) that activate the innate immune machinery upon detection of a cognate pathogen associated molecular pattern (PAMP). The RIG-I like receptor (RLR) family of PRRs includes three proteins — RIG-I, MDA5, and LGP2 — responsible for the detection of intracellular pathogenic RNA. All RLR proteins are built around an ATPase core homologous to those found in canonical Superfamily 2 (SF2) RNA helicases, which has been modified through the addition of novel accessory domains to recognize duplex RNA. This review focuses on the structural bases for pathogen-specific dsRNA binding and ATPase activation in RLRs, differential RNA recognition by RLR family members, and implications for other duplex RNA activated ATPases, such as Dicer.
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