人白细胞介素-1α的定点突变体：一项¹H-NMR和受体结合研究。
Site directed mutants of human interleukin-1 alpha: a 1H-NMR and receptor binding study.
作者信息
Gronenborn A M, Wingfield P T, McDonald H R, Schmeissner U, Clore G M
机构信息
Max-Planck-Institut für Biochemie, Martinsried bei München, FRG.
出版信息
FEBS Lett. 1988 Apr 11;231(1):135-8. doi: 10.1016/0014-5793(88)80717-8.
Mutant human interleukin-1 alpha proteins were constructed by oligonucleotide directed mutagenesis. Six different mutants were tested for receptor binding activity and showed no alteration with respect to the wild-type protein. Analysis of these mutants by nuclear magnetic resonance spectroscopy confirmed the structural integrity of the mutant proteins and permitted the sequence specific assignment of the histidine and tryptophan residues.
通过寡核苷酸定向诱变构建了突变型人白细胞介素-1α蛋白。对六种不同的突变体进行了受体结合活性测试，结果显示与野生型蛋白相比没有变化。通过核磁共振光谱对这些突变体进行分析，证实了突变蛋白的结构完整性，并实现了组氨酸和色氨酸残基的序列特异性归属。
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