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Publication Abstract from PubMed

The Toll/interleukin-1 receptor (TIR) domains are key innate immune signaling modules. Here, we present the crystal structure of the TIR domain of human Interleukin-1 receptor 10 (IL-1R10), also called IL-1RAPL2. It is similar to that of IL-1R9 (IL-1RAPL1) but shows significant structural differences to those from Toll-like receptors (TLRs) and the adaptor proteins MAL and MyD88. Interactions of TIR domains in their respective crystals and the higher-order assemblies (MAL and MyD88) reveal the presence of a common 'BCD surface', suggesting its functional significance. We also show that the TIR domains of IL-1R10 and IL-1R9 lack NADase activity, consistent with their structures. Our study provides a foundation for unraveling the functions of IL-1R9 and IL-1R10.

Crystal structure of the Toll/interleukin-1 receptor (TIR) domain of IL-1R10 provides structural insights into TIR domain signaling.,Nimma S, Gu W, Manik MK, Ve T, Nanson JD, Kobe B FEBS Lett. 2022 Jan 17. doi: 10.1002/1873-3468.14288. PMID:35038778^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.