Journal
FEBS LETTERS
Volume 594, Issue 15, Pages 2396-2405Publisher
WILEY
DOI: 10.1002/1873-3468.13866
Keywords
crystal structure; inflammasome; inflammation; NLRP9; PYD domain
Funding
- Basic Science Research Program of the National Research Foundation of Korea (NRF) of the Ministry of Education, Science, and Technology [NRF2017M3A9D8062960, NRF-2018R1A2B2003635]
- Korea Healthcare Technology RD Project
- Ministry of Health & Welfare, Republic of Korea [HI17C0155]
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Members of the NLR family pyrin domain containing (NLRPs) are pattern recognition receptors that participate in innate immunity. They form inflammasomes, which are platforms for caspase-1 recruitment and activation. The NLRP pyrin domain (PYD) is critical for the assembly of inflammasomes due to its ability to mediate protein interactions. Despite intensive structural studies on inflammasomes with PYDs, the structure of the PYD of NLRP9-the least studied member of the family-remains unknown. Herein, we report the crystal structure of the human NLRP9 PYD at 2.1 angstrom resolution, which reveals a kinked N-terminal loop oriented toward the interior of the helical bundle. Based on our findings, we propose a regulatory role for the kinked N-terminal loop of NLRP9 PYD in inflammasome assembly.
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