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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1998-6-4
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pubmed:abstractText |
A variant of human interferon-gamma (IFN-gamma) has been created in which the two chains of the homodimeric cytokine were linked N- to C-terminus by an eight residue polypeptide linker. The sequence of this linker was derived from a loop in bira bifunctional protein, and was determined from a structural database search. This "single-chain" variant was used to create an IFN-gamma molecule that binds only a single copy of the alpha-chain receptor, rather than the 2 alpha-chain receptor: 1 IFN-gamma binding stoichiometry observed for the native hormone. Crystals have been grown of a 1:1 complex between this single-chain molecule and the extracellular domain of its alpha-chain receptor. These crystals diffract beyond 2.0 A, significantly better than the 2.9 A observed for the native 2:1 complex. Density calculations suggest these crystals contain two complexes in the asymmetric unit; a self-rotation function confirms this conclusion.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-1409546,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-1830392,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-2059622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-2164668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-2475121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-2837824,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-3881765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-6173769,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-6180322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-6300774,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-6427223,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-7617032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-8124716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-8349687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-8476573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9568913-9048382
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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 |
Apr
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1057-60
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:9568913-Animals,
pubmed-meshheading:9568913-Cattle,
pubmed-meshheading:9568913-Crystallization,
pubmed-meshheading:9568913-Crystallography, X-Ray,
pubmed-meshheading:9568913-Dimerization,
pubmed-meshheading:9568913-Escherichia coli,
pubmed-meshheading:9568913-Humans,
pubmed-meshheading:9568913-Interferon-gamma,
pubmed-meshheading:9568913-Models, Molecular,
pubmed-meshheading:9568913-Molecular Weight,
pubmed-meshheading:9568913-Mutagenesis,
pubmed-meshheading:9568913-Protein Binding,
pubmed-meshheading:9568913-Protein Conformation,
pubmed-meshheading:9568913-Protein Structure, Secondary,
pubmed-meshheading:9568913-Receptors, Interferon,
pubmed-meshheading:9568913-Recombinant Proteins
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pubmed:year |
1998
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pubmed:articleTitle |
Crystallization and preliminary X-ray analysis of a 1:1 complex between a designed monomeric interferon-gamma and its soluble receptor.
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pubmed:affiliation |
Graduate Group in Biophysics, University of California, San Francisco 94000, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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