| Autor: |
de Hon FD; Department of Autoimmune Diseases, University of Amsterdam, The Netherlands., Klaasse Bos HK, Ebeling SB, Grötzinger J, Kurapkat G, Rose-John S, Aarden LA, Brakenhoff JP |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 1995 Aug 07; Vol. 369 (2-3), pp. 187-91. |
| DOI: |
10.1016/0014-5793(95)00741-q |
| Abstrakt: |
A model of the tertiary structure of human IL-6, derived from the crystal-structure of granulocyte-colony stimulating factor, reveals a 5th helical region in the loop between the first and second alpha-helix. To investigate the importance of this region for biological activity of IL-6, residues Glu-52, Ser-53, Ser-54, Lys-55, Glu-56, Leu-58, and Glu-60 were individually replaced by alanine. IL-6.Leu-58Ala displayed a 5-fold reduced biological activity on the IL-6 responsive human cell lines XG-1 and A375. This reduction in bioactivity was shown to be due to a decreased capacity of the mutant protein to trigger IL-6 receptor-alpha-chain-dependent binding to the IL-6 signal transducer, gp130. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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