Miedel M C, Hulmes J D, Weber D V, Bailon P, Pan Y C
Department of Protein Biochemistry, Roche Research Center, Hoffmann-La Roche Inc., Nutley, NJ.
Biochem Biophys Res Commun. 1988 Jul 15;154(1):372-9. doi: 10.1016/0006-291x(88)90695-x.
A purified soluble and functional form of recombinant human interleukin-2 receptor, engineered and expressed in Chinese hamster ovary cells, was structurally characterized. The primary sequence of this 224 amino acid recombinant protein which lacks most of the carboxy-terminal transmembrane and cytoplasmic portions of the intact protein was established by sequence analyses. The disulfide bonds were assigned by comparative peptide mapping of the reduced and non-reduced peptide digests. As in the case of natural interleukin-2 receptor they occur between cysteines 3-147, 46-104, 131-163, and 28/30-59/61. Based on assignment of the disulfide bonds, a structural model of the interleukin-2 receptor for interleukin-2 binding is proposed.
一种在中国仓鼠卵巢细胞中工程化表达的纯化的可溶性且具有功能的重组人白细胞介素-2受体，对其进行了结构表征。通过序列分析确定了这种由224个氨基酸组成的重组蛋白的一级序列，该蛋白缺乏完整蛋白大部分的羧基末端跨膜和细胞质部分。通过对还原和非还原肽消化产物的比较肽图谱分析确定了二硫键。与天然白细胞介素-2受体的情况一样，它们存在于半胱氨酸3-147、46-104、131-163以及28/30-59/61之间。基于二硫键的确定，提出了白细胞介素-2受体与白细胞介素-2结合的结构模型。
