Abstract：
Nucleotide-binding and leucine-rich repeat (NLR) proteins are critical intracellular immune receptors in both animals and plants. Perception of pathogen-derived or stress-associated signals induces NLR oligomerization to form multiprotein complexes called inflammasomes in animals or resistosomes in plants to mediate host immune response. Significant progress has been made during the past few years in our understanding of NLR biology, particularly the structural perspective of these two types of NLR-containing complexes. In this article, we review the latest advances in our structural knowledge of how NLR inflammasomes and resistosomes are activated and assembled and how the structural information provides insight into their distinct mechanisms of action. Commonalities and differences between NLR inflammasomes and resistosomes are also discussed.
摘要：
核苷酸结合和富含亮氨酸的重复（NLR）蛋白是动物和植物中关键的细胞内免疫受体。病原体来源或应激相关信号的感知诱导NLR寡聚化,以在动物中形成称为炎性体的多蛋白复合物或在植物中形成抗性体,以介导宿主免疫应答。在过去的几年中，我们对NLR生物学的理解取得了重大进展，特别是这两种类型的含NLR的复合物的结构观点。在这篇文章中,我们回顾了有关NLR炎性体和抵抗体如何激活和组装的结构知识的最新进展，以及结构信息如何提供对其独特作用机制的见解。还讨论了NLR炎性体和抗性体之间的共性和差异。生物物理学年度评论的预期最终在线出版日期，第52卷是2023年5月。请参阅http://www。annualreviews.org/page/journal/pubdates的订正估计数。
