Cryo-EM structure of the NLRC4^CARD filament provides insights into how symmetric and asymmetric supramolecular structures drive inflammasome assembly.

ABSTRACT: Inflammasomes are supramolecular signaling platforms integral to innate immune defense against invading pathogens. The NOD-like receptor (NLR) family apoptosis inhibitory protein (NAIP)·NLR family caspase-recruiting domain (CARD) domain-containing 4 (NLRC4) inflammasome recognizes intracellular bacteria and induces the polymerization of the caspase-1 protease, which in turn executes maturation of interleukin-1β (IL-1β) and pyroptosis. Several high-resolution structures of the fully assembled NAIP·NLRC4 complex are available, but these structures do not resolve the architecture of the CARD filament in atomic detail. Here, we present the cryo-EM structure of the filament assembled by the CARD of human NLRC4 (NLRC4^CARD) at 3.4 Å resolution. The structure revealed that the helical a

SUBMITTER: Matyszewski M 

PROVIDER: S-EPMC6311515 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature