炎症体
吡喃结构域
点头
化学
受体
细胞生物学
生物物理学
行动方式
环核苷酸结合域
核苷酸
生物化学
生物
基因
作者
Umeharu Ohto,Yukie Kamitsukasa,Hanako Ishida,Zhikuan Zhang,Kazuyasu Murakami,Chie Hirama,Sakiko Maekawa,Toshiyuki Shimizu
标识
DOI:10.1073/pnas.2121353119
摘要
SignificanceThe nucleotide-binding oligomerization domain (NOD)-like receptor pyrin domain containing 3 (NLRP3) is a pattern recognition receptor that forms an inflammasome. The cryo-electron microscopy structure of the dodecameric form of full-length NLRP3 bound to the clinically relevant NLRP3-specific inhibitor MCC950 has established the structural basis for the oligomerization-mediated regulation of NLRP3 inflammasome activation and the mechanism of action of the NLRP3 specific inhibitor. The inactive NLRP3 oligomer represents the NLRP3 resting state, capable of binding to membranes and is likely disrupted for its activation. Visualization of the inhibitor binding mode will enable optimization of the activity of NLRP3 inflammasome inhibitor drugs.
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