Zurawski S M, Zurawski G
Department of Molecular Biology, DNAX Research Institute, Palo Alto, CA 94304.
EMBO J. 1988 Apr;7(4):1061-9. doi: 10.1002/j.1460-2075.1988.tb02914.x.
We have analyzed structure--function relationships of the protein hormone murine interleukin 2 by fine structural deletion mapping. A total of 130 deletion mutant proteins, together with some substitution and insertion mutant proteins, was expressed in Escherichia coli and analyzed for their ability to sustain the proliferation of a cloned murine T cell line. This analysis has permitted a functional map of the protein to be drawn and classifies five segments of the protein, which together contain 48% of the sequence, as unessential to the biological activity of the protein. A further 26% of the protein is classified as important, but not crucial, for the activity. Three regions, consisting of amino acids 32-35, 66-77 and 119-141 contain the remaining 26% of the protein and are critical to the biological activity of the protein. The functional map is discussed in the context of the possible role of the identified critical regions in the structure of the hormone and its binding to the interleukin 2 receptor complex.
我们通过精细结构缺失图谱分析了蛋白质激素小鼠白细胞介素2的结构-功能关系。总共130种缺失突变蛋白，连同一些替代和插入突变蛋白，在大肠杆菌中表达，并分析它们维持克隆的小鼠T细胞系增殖的能力。该分析使得能够绘制该蛋白质的功能图谱，并将该蛋白质的五个区段（共包含48%的序列）归类为对该蛋白质的生物学活性无关紧要。该蛋白质另外26%被归类为对活性重要但非关键。由氨基酸32 - 35、66 - 77和119 - 141组成的三个区域包含该蛋白质其余26%，并且对该蛋白质的生物学活性至关重要。在已确定的关键区域在激素结构及其与白细胞介素2受体复合物结合中的可能作用的背景下讨论了功能图谱。
