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Mutational analysis of chicken interleukin 2.

机译:鸡白介素的突变分析2。

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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.
机译:鸡白介素2(chIL-2)与哺乳动物IL-2和哺乳动物IL-15同源性低,但意义重大。鉴于其独特的系统发育位置和作为疫苗佐剂的潜在用途,对关键功能位点进行了详细的突变分析。发现Asp17是与假定的chIL-2受体结合的关键N末端接触位点,这与哺乳动物IL-2和IL-15获得的结果相似。 C末端的分析未揭示单个关键氨基酸。但是,缺失突变体研究表明,去除C末端氨基酸会产生具有降低的生物活性的蛋白质,并且这种减少是所去除氨基酸的数量和种类的函数。这项研究是首次非哺乳动物IL-2突变分析,并提出了chIL-2及其受体之间相互作用的模型。版权所有2001,学术出版社。

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