| pubmed-article:8401231 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8401231 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:8401231 | lifeskim:mentions | umls-concept:C0021760 | lld:lifeskim |
| pubmed-article:8401231 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8401231 | lifeskim:mentions | umls-concept:C0026377 | lld:lifeskim |
| pubmed-article:8401231 | lifeskim:mentions | umls-concept:C0205360 | lld:lifeskim |
| pubmed-article:8401231 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:8401231 | pubmed:dateCreated | 1993-11-23 | lld:pubmed |
| pubmed-article:8401231 | pubmed:abstractText | Two murine interleukin-6 (mIL-6) variants were constructed using the polymerase chain reaction (PCR), one lacking the last five residues (183-187) at the C-terminus (pMC5) and another with the last five residues of mIL-6 substituted by the corresponding residues of human IL-6 (pMC5H). The growth stimulatory activity of pMC5 on the mouse hybridoma cell line 7TD1 was < 0.05% of mIL-6, whereas pMC5H and mIL-6 were equipotent. The loss of biological activity of pMC5 correlated with its negligible receptor binding affinity on 7TD1 cells, while the binding of pMC5H was comparable to that of mIL-6. Both pMC5 and pMC5H, like mIL-6, failed to interact with recombinant soluble human IL-6 receptor when assayed by surface plasmon resonance-based biosensor analysis. These studies suggest that the C-terminal seven amino acids of human IL-6, alone, do not define species specificity for receptor binding. A variety of biophysical techniques, as well as the binding of a conformational-specific monoclonal antibody, indicated that the global fold of the mIL-6 variants was similar to that of mIL-6, although small changes in the NMR spectra, particularly for pMC5, were observed. Some of these changes involved residues widely separated in the primary structure. For instance, interactions involving Tyr-22 were influenced by the C-terminal amino acids suggesting that the N- and C-termini of mIL-6 are in close proximity. Equilibrium unfolding experiments indicated that pMC5 was 0.8 kcal/mol less stable than mIL-6, whereas pMC5H was 1.4 kcal/mol more stable. These studies emphasize the structural importance of the C-terminal amino acids of IL-6 and suggest that truncation or mutation of this region could lead to small but significant alterations in other regions of the molecule. | lld:pubmed |
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| pubmed-article:8401231 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8401231 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8401231 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8401231 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8401231 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8401231 | pubmed:issn | 0961-8368 | lld:pubmed |
| pubmed-article:8401231 | pubmed:author | pubmed-author:SimpsonR JRJ | lld:pubmed |
| pubmed-article:8401231 | pubmed:author | pubmed-author:NortonR SRS | lld:pubmed |
| pubmed-article:8401231 | pubmed:author | pubmed-author:YasukawaKK | lld:pubmed |
| pubmed-article:8401231 | pubmed:author | pubmed-author:MortonC JCJ | lld:pubmed |
| pubmed-article:8401231 | pubmed:author | pubmed-author:WeinstockJJ | lld:pubmed |
| pubmed-article:8401231 | pubmed:author | pubmed-author:ZhangJ GJG | lld:pubmed |
| pubmed-article:8401231 | pubmed:author | pubmed-author:HammacherAA | lld:pubmed |
| pubmed-article:8401231 | pubmed:author | pubmed-author:WardL DLD | lld:pubmed |
| pubmed-article:8401231 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8401231 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:8401231 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8401231 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8401231 | pubmed:pagination | 1472-81 | lld:pubmed |
| pubmed-article:8401231 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:8401231 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8401231 | pubmed:articleTitle | Role of the C-terminus in the activity, conformation, and stability of interleukin-6. | lld:pubmed |
| pubmed-article:8401231 | pubmed:affiliation | Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research, Parkville, Victoria, Australia. | lld:pubmed |
| pubmed-article:8401231 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8401231 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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