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Nature. 1995 Jul 20;376(6537):217-8.
Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor.
Department of Pharmacology, University of Alabama at Birmingham 35294, USA.
The crystal structure of interferon-gamma bound to the extracellular fragment of its high-affinity cell-surface receptor reveals the first view of a class-2 cytokine receptor-ligand complex. In the complex, one interferon-gamma homodimer binds two receptor molecules. Unlike the class-1 growth hormone receptor complex, the two interferon-gamma receptors do not interact with one another and are separated by 27 A. Upon receptor binding, the flexible AB loop of interferon-gamma undergoes a conformational change that includes the formation of a 3(10) helix.
PMID: 7617032 [PubMed - indexed for MEDLINE]
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Cited by 35 PubMed Central articles
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Structure and mechanism of IFN-gamma antagonism by an orthopoxvirus IFN-gamma-binding protein.
Nuara AA, Walter LJ, Logsdon NJ, Yoon SI, Jones BC, Schriewer JM, Buller RM, Walter MR.
Proc Natl Acad Sci U S A. 2008 Feb 12; 105(6):1861-6. Epub 2008 Feb 5.
[Proc Natl Acad Sci U S A. 2008]
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The EM structure of a type I interferon-receptor complex reveals a novel mechanism for cytokine signaling.
Li Z, Strunk JJ, Lamken P, Piehler J, Walz T.
J Mol Biol. 2008 Mar 28; 377(3):715-24. Epub 2007 Dec 8.
[J Mol Biol. 2008]
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Interleukin-22 forms dimers that are recognized by two interleukin-22R1 receptor chains.
de Oliveira Neto M, Ferreira JR Jr, Colau D, Fischer H, Nascimento AS, Craievich AF, Dumoutier L, Renauld JC, Polikarpov I.
Biophys J. 2008 Mar 1; 94(5):1754-65. Epub 2007 Nov 16.
[Biophys J. 2008]
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