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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
37
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pubmed:dateCreated |
1994-10-11
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pubmed:abstractText |
The high affinity human interleukin-6 (IL-6) receptor complex consists of IL-6 and two membrane-associated receptor components, the IL-6 receptor (alpha-subunit) and the high affinity converter and signal transducing molecule, gp-130 (beta-subunit). Recombinant IL-6 and the extracellular ("soluble") components of the IL-6 receptor (sIL-6R) and gp-130 (sgp-130) have been prepared in order to investigate the stoichiometry and binding of these components in the low affinity (IL-6.sIL-6R) and high affinity (IL-6.sIL-6R.sgp-130) IL-6 receptor complexes. Using a combination of size-exclusion chromatography and analytical ultracentrifugation analysis, in the low affinity receptor complex, IL-6 was shown to bind sIL-6R in a stoichiometric ratio of 1:1, whereas the high affinity ternary complex is hexameric consisting of two molecules each of IL-6, sIL-6R, and sgp-130. This is the first direct demonstration of a higher order arrangement for receptor cytokine interactions that exhibit both high and low affinity complexes.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Cytokine Receptor gp130,
http://linkedlifedata.com/resource/pubmed/chemical/IL6ST protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-6,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
269
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
23286-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8083235-Amino Acid Sequence,
pubmed-meshheading:8083235-Antigens, CD,
pubmed-meshheading:8083235-Chromatography, Gel,
pubmed-meshheading:8083235-Cytokine Receptor gp130,
pubmed-meshheading:8083235-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:8083235-Humans,
pubmed-meshheading:8083235-Interleukin-6,
pubmed-meshheading:8083235-Membrane Glycoproteins,
pubmed-meshheading:8083235-Molecular Sequence Data,
pubmed-meshheading:8083235-Molecular Weight,
pubmed-meshheading:8083235-Receptors, Interleukin,
pubmed-meshheading:8083235-Receptors, Interleukin-6,
pubmed-meshheading:8083235-Recombinant Proteins,
pubmed-meshheading:8083235-Signal Transduction,
pubmed-meshheading:8083235-Ultracentrifugation
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pubmed:year |
1994
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pubmed:articleTitle |
High affinity interleukin-6 receptor is a hexameric complex consisting of two molecules each of interleukin-6, interleukin-6 receptor, and gp-130.
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pubmed:affiliation |
Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research (Melbourne), Walter and Eliza Hall Institute of Medical Research, Royal Melbourne Hospital, Parkville, Victoria, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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