Crystal structure of a complex between interferon-γ and its soluble high-affinity receptor

• Published in: Nature (London) 1995-07, Vol.376 (6537), p.230-235
• Main Authors: Walter, Mark R, Windsor, William T, Nagabhushan, Tattanahalli L, Lundell, Daniel J, Lunn, Charles A, Zauodny, Paul J, Narula, Satwant K
• Format: Article
• Language: English
• Subjects: Biological and medical sciences; Cell receptors; Cell structures and functions; Computer Graphics; Crystallography; Crystallography, X-Ray; Cytokines - chemistry; Escherichia coli; Fundamental and applied biological sciences. Psychology; Glycosylation; Growth Hormone - chemistry; Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors; Humanities and Social Sciences; Humans; Interferon; Interferon gamma Receptor; Interferon-gamma - chemistry; Molecular and cellular biology; Molecular biology; multidisciplinary; Protein Conformation; Receptors, Interferon - chemistry; Receptors, Somatotropin - chemistry; Recombinant Proteins - chemistry; Science; Science (multidisciplinary); Solubility
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/376230a0

The crystal structure of interferon-γ bound to the extracellular fragment of its high-affinity cellsurface receptor reveals the first view of a class-2 cytokine receptor-ligand complex. In the complex, one interferon-γ homodimer binds two receptor molecules. Unlike the class-1 growth hormone receptor complex, the two interferon-γ receptors do not interact with one another and are separated by 27 Ã. Upon receptor binding, the flexible AB loop of interferon-γ undergoes a conformational change that includes the formation of a 3 10 helix.