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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6537
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pubmed:dateCreated |
1995-8-22
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pubmed:abstractText |
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.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
376
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
230-5
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:7617032-Computer Graphics,
pubmed-meshheading:7617032-Crystallography, X-Ray,
pubmed-meshheading:7617032-Cytokines,
pubmed-meshheading:7617032-Escherichia coli,
pubmed-meshheading:7617032-Glycosylation,
pubmed-meshheading:7617032-Growth Hormone,
pubmed-meshheading:7617032-Humans,
pubmed-meshheading:7617032-Interferon-gamma,
pubmed-meshheading:7617032-Protein Conformation,
pubmed-meshheading:7617032-Receptors, Interferon,
pubmed-meshheading:7617032-Receptors, Somatotropin,
pubmed-meshheading:7617032-Recombinant Proteins,
pubmed-meshheading:7617032-Solubility
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pubmed:year |
1995
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pubmed:articleTitle |
Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor.
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pubmed:affiliation |
Department of Pharmacology, University of Alabama at Birmingham 35294, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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