Site-specific mutagenesis of the human interleukin-2 gene: structure-function analysis of the cysteine residues.
Site-specific mutagenesis of the human interleukin-2 gene: structure-function analysis of the cysteine residues.
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人白细胞介素 2 基因的位点特异性诱变：半胱氨酸残基的结构功能分析。
DOI：
10.1126/science.6427925
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发表时间：
1984
期刊：
影响因子：
56.9
通讯作者：
D. Mark
中科院分区：
文献类型：
--
作者：
A. Wang;S. D. Lu;D. Mark
已从人脾细胞、外周血淋巴细胞和Jurkat细胞系中克隆了编码人白细胞介素-2（IL-2）的基因。对该基因的核苷酸序列分析显示，编码的IL-2蛋白具有三个半胱氨酸，分别位于成熟蛋白的氨基酸残基58、105和125处。使用位点特异性诱变程序通过将每个半胱氨酸密码子单独改变为丝氨酸密码子来修饰IL-2基因。在IL-2蛋白的58或105位用丝氨酸取代半胱氨酸残基基本上降低了生物活性，表明这些位置的半胱氨酸对于维持生物活性构象是必需的，因此可能通过二硫桥连接。在位置125处含有取代的修饰的IL-2蛋白保留了完全的生物活性，表明在该位置处的半胱氨酸不参与二硫键，并且在该位置处的游离巯基对于受体结合不是必需的。
The gene encoding human interleukin-2 (IL-2) has been cloned from human spleen cells, peripheral blood lymphocytes, and the Jurkat cell line. Nucleotide sequence analysis of the gene revealed that the encoded IL-2 protein has three cysteines located at amino acid residues 58, 105, and 125 of the mature protein. Site-specific mutagenesis procedures were used to modify the IL-2 gene by changing each of the cysteine codons individually to serine codons. Substitution of serine for cysteine residues at either position 58 or 105 of the IL-2 protein substantially reduced biological activity, indicating that the cysteines at these positions are necessary for maintenance of the biologically active conformation and may therefore be linked by a disulfide bridge. The modified IL-2 protein containing a substitution at position 125 retained full biological activity, suggesting that the cysteine at this position is not involved in a disulfide bond and that a free sulfhydryl group at that position is not necessary for receptor binding.
人 T 细胞生长因子：纯化生化特性以及与细胞受体的相互作用。
影响因子：
2.8
作者：
Robb,RJ
通讯作者：
Robb,RJ