Abstract:
:Interleukin 1 (IL-1) is a two-member family of proteins (IL-1 alpha and IL-1 beta) that mediates a diverse series of immune and inflammatory responses. These two proteins have only 26% amino acid homology yet bind to the same receptor. It is of importance to define the active sites of these molecules in order to understand their receptor interactions and the mechanisms involved in their multiple biological functions. We report here the localization of the biologically active portions within the initial polypeptide translation products. An in vitro transcription and translation system was used to generate specific fragments of each of the IL-1 molecules, which then were assayed for receptor binding capability and biological activity. Using this system, we have demonstrated that core sequences of amino acids for IL-1 beta (numbers 120-266) and 140 amino acids for IL-1 alpha (numbers 128-267) must be left intact to retain full biological activity and further that the biological activities of the IL-1 polypeptides parallel their receptor binding capabilities.
journal_name
Proc Natl Acad Sci U S Aauthors
Mosley B,Dower SK,Gillis S,Cosman Ddoi
10.1073/pnas.84.13.4572subject
Has Abstractpub_date
1987-07-01 00:00:00pages
4572-6issue
13eissn
0027-8424issn
1091-6490journal_volume
84pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:2001-11-20 00:00:00
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:1997-11-25 00:00:00