Comment
doi: 10.1016/j.tibs.2022.03.014.
Epub 2022 Apr 2.
NLRP3 is its own gatekeeper: a group hug of NLRP3 monomers controls inflammation
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- PMID: 35382945
- DOI: 10.1016/j.tibs.2022.03.014
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Comment
NLRP3 is its own gatekeeper: a group hug of NLRP3 monomers controls inflammation
Trends Biochem Sci.
2022 Aug.
Abstract
A recent study by Hochheiser et al. describes the cryo-electron microscopy (cryoEM) structure of an autoinhibited nucleotide-binding domain-, leucine-rich repeat (LRR)- and pyrin domain-containing protein 3 (NLRP3) decamer that assembles via LRR interactions and is further stabilized by the small-molecule NLRP3-specific inhibitor CRID3 binding into a cleft within the NACHT domain. The study provides a springboard for the development of novel NLRP3-based therapies.
Keywords: CRID3; Inflammasome; MCC950; NLRP3; inhibitor; oligomer.
Copyright © 2022 Elsevier Ltd. All rights reserved.
Conflict of interest statement
Declaration of interests I.H.-B. has no competing interests to declare.
Comment on
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Structure of the NLRP3 decamer bound to the cytokine release inhibitor CRID3.Nature. 2022 Apr;604(7904):184-189. doi: 10.1038/s41586-022-04467-w. Epub 2022 Feb 3. Nature. 2022. PMID: 35114687
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