Structural insights into the assembly and activation of IL-1β with its receptors

Wang, Dongli; Zhang, Senyan; Li, Liang; Liu, Xi; Mei, Kunrong; Wang, Xinquan

doi:10.1038/ni.1925

Cited by 162Cytokine Signaling Pathways and InteractionsInflammasome and immune disordersImmune Response and Inflammation

Structural insights into the assembly and activation of IL-1β with its receptors

Wang, Dongli, Zhang, Senyan, Li, Liang, Liu, Xi, Mei, Kunrong, Wang, Xinquan·2010·Nature Immunology

DOI 10.1038/ni.1925

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Abstract

Interleukin 1β (IL-1β) is a key orchestrator of inflammation and host defense that exerts its effects through IL-1 receptor type I (IL-1RI) and IL-1 receptor accessory protein (IL-1RAcP). How IL-1RAcP is recruited by IL-1β-IL-1RI to form the signaling-competent complex remains elusive. Here we present the crystal structure of IL-1β bound to IL-1 receptor type II (IL-1RII) and IL-1RAcP. IL-1β-IL-1RII generated a composite binding surface to recruit IL-1RAcP. Biochemical analysis demonstrated that IL-1β-IL-1RI and IL-1β-IL-1RII interacted similarly with IL-1RAcP. It also showed the importance of two loops of IL-1 receptor antagonist (IL-1Ra) in determining its antagonism. Our results provide a structural basis for assembly and activation of the IL-1 receptor and offer a general cytokine-receptor architecture that governs the IL-1 family of cytokines.

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rTregs subset expressed higher levels of quiescence genes Ms4a4b and Sell, whereas aTregs subset expressed higher levels of coinhibitory Pdcd1 and Lag3, costimulatory Tnfrsf9 and Tnfrsf4, activation genes S100a11 and Il1r2, and TF Ikzf2.
“whereas the rTregs subset expressed higher levels of quiescence genes (e.g., Ms4a4b and Sell), aTregs subset expressed higher levels of coinhibitory (e.g., Pdcd1 and Lag3) and costimulatory genes [e.g., Tnfrsf9 and Tnfrsf4; (38)], activation genes [S100a11 and Il1r2 (IL1 decoy receptor); (39)], and the transcription factor (TF) Ikzf2 (30).”
From Aging promotes reorganization of the CD4 T cell landscape toward extreme regulatory and effector phenotypes (2019) · cites this paper as [39]

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Authors: Wang, D., Zhang, S., Li, L., Liu, X., Mei, K., & Wang, X.
Affiliations: Tsinghua University (CN)
ORCID: Wang, Dongli
Zhang, Senyan
Li, Liang
Liu, Xi
Mei, Kunrong
Wang, Xinquan
Venue: Nature Immunology
Publisher: Springer Science and Business Media LLC
Published: 2010-08-29
Volume: 11
Issue: 10
Pages: 905-911
ISSN: 1529-2908 (ISSN-L)
1529-2916
DOI: 10.1038/ni.1925
OpenAlex: W2128418292
Cited by: 162
References: 54
Citations by year: 2026: 6 · 2025: 12 · 2024: 5 · 2023: 8 · 2022: 14 · 2021: 8 · 2020: 9 · 2019: 13 · 2018: 9 · 2017: 8 · 2016: 13 · 2015: 12 · 2014: 13 · 2013: 19 · 2012: 7
FWCI: 5.07
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Immunology (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords: IL-1β, IL-1 receptor type I, IL-1 receptor accessory protein, receptor activation, interleukin-1 receptor antagonist, crystal structure, IL-1 family cytokines, inflammation
MeSH terms: Amino Acid Sequence, Crystallography, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Signal Transduction, Sequence Alignment, Protein Structure, Tertiary, Receptors, Interleukin-1 Type II, Interleukin-1 Receptor Accessory Protein, Interleukin-1beta, Interleukin 1 Receptor Antagonist Protein

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Structural insights into the assembly and activation of IL-1β with its receptors

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