The full form of NLRs is Nucleotide-binding oligomerization domain-like receptors.
NLRs, also known as nucleotide-binding leucine-rich repeat receptors, are a crucial part of the innate immune system. They function as intracellular sensors that detect pathogen-associated molecular patterns (PAMPs) and damage-associated molecular patterns (DAMPs). These patterns enter the cell through processes like phagocytosis or via pores in the cell membrane.
Here's a breakdown:
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Nucleotide-binding: This refers to the domain within the receptor that binds to nucleotides, which are essential molecules for energy transfer and signaling within cells.
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Oligomerization domain: This domain allows multiple NLR molecules to come together (oligomerize) upon activation, forming a larger complex that triggers downstream signaling pathways.
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Like receptors: NLRs are similar in structure and function to other pattern recognition receptors like Toll-like receptors (TLRs), which are located on the cell surface.
NLRs play a critical role in initiating inflammatory responses and activating pathways such as the inflammasome, which leads to the release of cytokines that fight infection and promote tissue repair.
