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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-6-16
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pubmed:abstractText |
Interleukin-6 (IL-6) is a 185 amino acid cytokine which exerts multiple biological effects in vivo and whose dysregulation underlies several disease processes. The solution structure of recombinant human interleukin-6 has now been determined using heteronuclear three and four-dimensional NMR spectroscopy. The structure of the molecule was determined using 3044 distance and torsion restraints derived by NMR spectroscopy to generate an ensemble of 32 structures using a combined distance geometry/simulated annealing protocol. The protein contains five alpha-helices interspersed with variable-length loops; four of these helices constitute a classical four-helix bundle with the fifth helix located in the CD loop. There were no distance violations greater than 0.3 A in any of the final 32 structures and the ensemble has an average-to-the-mean backbone root-mean-square deviation of 0.50 A for the core four-helix bundle. Although the amino-terminal 19 amino acids are disordered in solution, the remainder of the molecule has a well defined structure that shares many features displayed by other long-chain four-helix bundle cytokines. The high-resolution NMR structure of hIL-6 is used to rationalize available mutagenesis data in terms of a heteromeric receptor complex.
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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/Interleukin-6,
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,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0022-2836
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
2
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
468-81
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:9159484-Antigens, CD,
pubmed-meshheading:9159484-Binding Sites,
pubmed-meshheading:9159484-Humans,
pubmed-meshheading:9159484-Hydrogen Bonding,
pubmed-meshheading:9159484-Interleukin-6,
pubmed-meshheading:9159484-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9159484-Models, Molecular,
pubmed-meshheading:9159484-Mutagenesis,
pubmed-meshheading:9159484-Protein Binding,
pubmed-meshheading:9159484-Protein Structure, Secondary,
pubmed-meshheading:9159484-Protein Structure, Tertiary,
pubmed-meshheading:9159484-Receptors, Interleukin,
pubmed-meshheading:9159484-Receptors, Interleukin-6,
pubmed-meshheading:9159484-Recombinant Proteins,
pubmed-meshheading:9159484-Solutions,
pubmed-meshheading:9159484-Structure-Activity Relationship
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pubmed:year |
1997
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pubmed:articleTitle |
Solution structure of recombinant human interleukin-6.
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pubmed:affiliation |
Small Molecule Drug Discovery, Genetics Institute, Cambridge, MA 02140, USA.
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pubmed:publicationType |
Journal Article
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