meRfi®-GM
Toll-interleukin-1 receptor (TIR) homology domain
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Contents
The Toll-interleukin-1 receptor (TIR) homology domains were initially identified as modules facilitating protein-protein interactions in Toll-like receptors (TLRs) and interleukin-1 receptors, as noted by Takeda and Akira (2025). Additionally, these domains are recognized as the N-terminal domain of certain plant NLRs, as discussed by Barragan and Weigel (2021).
Recently, it was discovered that multiple Toll-interleukin-1 receptor (TIR) homology domains throughout the tree of life exhibit a shared enzymatic activity, specifically that of [Nicotinamide dinucleotide hydrolase (NADase)](brain://AvjCXYioj0W-z_…
References (Sources)
- Plant NLR diversity: the known unknowns of pan-NLRomes
- Shared TIR enzymatic functions regulate cell death and immunity across the tree of life
- The SARM1 Toll/interleukin-1 receptor domain possesses intrinsic NAD+ cleavage activity that promotes pathological axonal degeneration
- TIR Domain Proteins Are an Ancient Family of NAD+ - Consuming Enzymes
- TIR domains of plant immune receptors are NAD+-cleaving enzymes that promote cell death
- Toll-like receptors in innate immunity.