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以人生长激素受体（Ｋ５２－Ｌ２５１）的晶体结构为模板，同源模建人白细胞介素－６ 受体（ｈＩＬ－６Ｒ）（Ｖ１０６－Ｐ３２２）的空间结构，并预测与配基（ＩＬ－６）结合的活性部位．根据 ｈＩＬ－６Ｒ配基结合功能域中重要氨基酸点突变对活性部位空间构象的影响，验证预测部 位的正确性．理论分析表明，ｈＩＬ－６Ｒ配基结合功能域中４个保守的半胱氨酸（Ｃｙｓ），近膜 侧１９３位Ｃｙｓ及“ＷＳＥＷＳ”主型框架的点突变均导致受体与配基的结合受阻；而２１１ 位Ｃｙｓ，２７７位Ｃｙｓ点突变却有利于受体与配基的结合．研究结果提示，预测的ｈＩＬ－６Ｒ 的活性部位确是ｈＩＬ－６Ｒ和配基（ＩＬ－６）结合的分子基础，可以作为进行小分子ｈＩＬ－６Ｒ拮 抗剂设计的靶部位。
The spatial structure of human interleukin-6 receptor (hIL-6R) (V106-P322) was homologously modeled by the crystal structure of human growth hormone receptor (K52-L251) -6) binding active site. According to hIL-6R ligand binding domain of important amino acid point mutation on the active site spatial conformation, verify the correctness of the predicted site. Theoretical analysis shows that point mutations in the four conserved cysteines (Cys), the 193-mesenchymal Cys, and the “WSEWS” mainframe in the hIL-6R ligand-binding domain both result in receptor-ligand binding Blocked; 211 Cys, 277 Cys point mutation is conducive to receptor and ligand binding. The results suggest that the predicted active site of hIL-6R is indeed the molecular basis of hIL-6R and ligand (IL-6) binding, and can be used as a target site for the design of small molecule hIL-6R antagonist.