| Literature DB >> 11292314 |
J E Kolodsick1, J A Stepaniak, W Hu, R S Sundick.
Abstract
Chicken interleukin 2 (chIL-2) has low, but significant, homology to both mammalian IL-2 and mammalian IL-15. In view of its unique phylogenetic position and potential use as a vaccine adjuvant, a detailed mutational analysis for critical functional sites was undertaken. It was found that Asp17 is a critical N terminal contact site for binding to the putative chIL-2 receptor, which is similar to results obtained for mammalian IL-2 and IL-15. Analysis of the C terminus did not reveal a single critical amino acid. However, deletion mutant studies demonstrated that removal of C terminal amino acids yielded proteins with decreased bioactivity and that this decrease was a function of the number and kind of amino acids removed. This study is the first non-mammalian IL-2 mutational analysis and proposes a model for the interaction between chIL-2 and its receptor. Copyright 2001 Academic Press.Entities:
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Year: 2001 PMID: 11292314 DOI: 10.1006/cyto.2001.0846
Source DB: PubMed Journal: Cytokine ISSN: 1043-4666 Impact factor: 3.861