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NOD-like receptor
The nucleotide-binding oligomerization domain receptors, in short NOD-like receptors (NLRs) are intracellular sensors of PAMPs that enter the cell via phagocytosis or pores and DAMPs that are associated with cell stress. They are part of pattern recognition receptors and play key roles in regulation of innate immune response. NLRs can cooperate with Toll-like receptors and regulate inflammatory and apoptotic response. They are found in lymphocytes, macrophages, dendritic cells and also in nonimmune cells, for example in epithelium. NLRs are highly conserved through evolution. Their homologs have been discovered in many different animal species (APAF1) and also in the plant kingdom (disease-resistance R protein).〔
==Structure==
NLRs contain 3 domains – central NACHT (NOD or NBD – nucleotide-binding domain) domain, which is common to all NLRs, most of NLRs have also C-terminal leucine-rich repeat (LRR) and variable N-terminal interaction domain. NACHT domain mediates ATP-dependent self-oligomerization and LRR senses the presence of ligand. N-terminal domain is responsible for homotypic protein-protein interaction and it can consist of caspase recruitment domain (CARD), pyrin domain (PYD), acidic transactivating domain or baculovirus inhibitor repeats (BIRs).〔
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