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• W4310366847 abstract "The family of human nucleotide-binding oligomerization domain (NOD) receptors comprises 22 members. NOD-like receptors (NLRs) share a similar domain architecture consisting of an N-terminal effector domain, a central regulatory domain, and the C-terminal sensory domain. Upon activation, some NLRs have been shown to form supramolecular complexes termed inflammasomes. These large cytosolic assemblies form within minutes after recognizing their specific triggers. They regulate the activation of highly proinflammatory cytokines and induce pyroptotic cell death. In this chapter, we present the conserved sequence motifs of the NLR family, the composition of the domain and subdomain structure, and the assembly into inactive and active states. Our current understanding of the transition from an autoinhibited conformation to a signaling-competent state is illustrated using the protein structures of NLRC4, NOD2, and NLRP3. The downstream effector functions of NLRs as nucleation seeds for homotypic PYD and caspase activation recruitment domain filament assemblies are discussed. These first insights raise the question of whether all NLRs function according to a similar mechanism and whether targeted inhibition of their regulation appears feasible for the specific treatment of inflammatory diseases." @default.
• W4310366847 created "2022-12-09" @default.
• W4310366847 creator A5068603027 @default.
• W4310366847 creator A5070130099 @default.
• W4310366847 date "2023-01-01" @default.
• W4310366847 modified "2023-09-26" @default.
• W4310366847 title "Structural aspects of inflammasomes forming NOD-like receptors" @default.
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• W4310366847 doi "https://doi.org/10.1016/b978-0-323-91802-2.00022-0" @default.
• W4310366847 hasPublicationYear "2023" @default.
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