Structural analysis of recombinant soluble human interleukin-2 receptor. Primary structure, assignment of disulfide bonds and core IL-2 binding structure.
Structural analysis of recombinant soluble human interleukin-2 receptor. Primary structure, assignment of disulfide bonds and core IL-2 binding structure.
复制标题
重组可溶性人白细胞介素2受体的结构分析。
DOI：
10.1016/0006-291x(88)90695-x
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发表时间：
1988
影响因子：
3.1
通讯作者：
Y. Pan
中科院分区：
文献类型：
--
作者：
M. Miedel;J. Hulmes;D. Weber;P. Bailon;Y. Pan
对重组人白介素2受体的结构进行了鉴定，并在中国仓鼠卵巢细胞中进行了表达。通过序列分析确定了该重组蛋白的一级序列，该重组蛋白缺少完整蛋白的大部分羧基末端、跨膜和胞质部分。二硫键是通过还原和非还原的多肽酶的比较肽图确定的。与天然白介素2受体的情况一样，它们出现在半胱氨酸3-147、46-104、131-163和28 30-59 61之间。基于二硫键的指认，提出了白介素2受体与白介素2结合的结构模型。
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.