Structural biology of the IL‐1 superfamily: Key cytokines in the regulation of immune and inflammatory responses

• Published in: Protein science Vol. 23; no. 5; pp. 526 - 538
• Main Authors: Krumm, Brian, Xiang, Yan, Deng, Junpeng
• Format: Journal Article
• Language: English
• Published: United States Wiley Subscription Services, Inc 01.05.2014; Wiley-Blackwell
• Subjects: agonist; Animals; antagonist; Crystallography, X-Ray; cytokine; Cytokines; Humans; inflammation; Inflammation - drug therapy; Inflammation - immunology; Intercellular Signaling Peptides and Proteins - chemistry; Intercellular Signaling Peptides and Proteins - immunology; interleukin; Interleukin 1 Receptor Antagonist Protein - chemistry; Interleukin 1 Receptor Antagonist Protein - immunology; Interleukin-1 - antagonists & inhibitors; Interleukin-1 - chemistry; Interleukin-1 - immunology; Interleukin-18 - chemistry; Interleukin-18 - immunology; Medical research; Models, Molecular; Protein Conformation; receptors; Reviews; Signal Transduction; cytokine; agonist; receptors; interleukin; inflammation; antagonist
• ISSN: 0961-8368; 1469-896X
• DOI: 10.1002/pro.2441

Interleukin‐1 superfamily of cytokines (IL‐1, IL‐18, IL‐33) play key roles in inflammation and regulating immunity. The mechanisms of agonism and antagonism in the IL‐1 superfamily have been pursued by structural biologists for nearly 20 years. New insights into these mechanisms were recently provided by the crystal structures of the ternary complexes of IL‐1β and its receptors. We will review here the structural biology related to receptor recognition by IL‐1 superfamily cytokines and the regulation of its cytokine activities by antagonists.