7SZL
Crystal structure of the Toll/interleukin-1 receptor domain of human IL-1R10 (IL-1RAPL2)
Summary for 7SZL
| Entry DOI | 10.2210/pdb7szl/pdb |
| Descriptor | X-linked interleukin-1 receptor accessory protein-like 2 (2 entities in total) |
| Functional Keywords | membrane protein, tir domain, interleukin-1 receptor, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 18919.92 |
| Authors | Nimma, S.,Gu, W.,Manik, M.K.,Ve, T.,Nanson, J.D.,Kobe, B. (deposition date: 2021-11-28, release date: 2022-02-02, Last modification date: 2023-10-18) |
| Primary citation | Nimma, S.,Gu, W.,Manik, M.K.,Ve, T.,Nanson, J.D.,Kobe, B. Crystal structure of the Toll/interleukin-1 receptor (TIR) domain of IL-1R10 provides structural insights into TIR domain signalling. Febs Lett., 596:886-897, 2022 Cited by PubMed 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. PubMed: 35038778DOI: 10.1002/1873-3468.14288 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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