Structural basis for the oligomerization-mediated regulation of NLRP3 inflammasome activation
Copyright policy )Structural basis for the oligomerization-mediated regulation of NLRP3 inflammasome activation
Significance The 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.
- University of Tokyo Japan
Models, Molecular, Mice, Structure-Activity Relationship, Binding Sites, Inflammasomes, Protein Conformation, Cryoelectron Microscopy, Mutation, NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Biological Sciences, Protein Multimerization, Protein Binding
Models, Molecular, Mice, Structure-Activity Relationship, Binding Sites, Inflammasomes, Protein Conformation, Cryoelectron Microscopy, Mutation, NLR Family, Pyrin Domain-Containing 3 Protein, Animals, Biological Sciences, Protein Multimerization, Protein Binding
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