In:
FEBS Letters, Wiley, Vol. 596, No. 7 ( 2022-04), p. 886-897
Abstract:
The Toll/interleukin‐1 receptor (TIR) domains are key innate immune signalling modules. Here, we present the crystal structure of the TIR domain of human interleukin‐1 receptor 10 (IL‐1R10), also called interleukin 1 receptor accessory protein like 2. 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 MyD88 adaptor‐like protein (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 unravelling the functions of IL‐1R9 and IL‐1R10.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1002/1873-3468.14288
Language:
English
Publisher:
Wiley
Publication Date:
2022
detail.hit.zdb_id:
1460391-3
SSG:
12
