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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A mixed-charge pair in human interleukin 4 dominates high-affinity interaction with the receptor α chain
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A mixed-charge pair in human interleukin 4 dominates high-affinity interaction with the receptor α chain

机译:人白介素4中的混合电荷对控制与受体α链的高亲和力相互作用

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摘要

Human interleukin 4 (IL-4) binds to its cellular receptor with a K_d in the subnanomolar range, similar to many other 4-helix-bundle proteins interacting with mem- bers of the hematopoietin (cytokine) receptor superfamily. In the IL-4 system this interaction is predominantly determined by the extracellular domain (IL4-BP) of the receptor chain (K_d ≈ 150 pM). Now a high-resolution mutational and kinetic analysis has revealed that the high-affinity binding of IL-4 originates from a continuous patch of a few mostly polar or charged amino acid side chains located on helices A and C.
机译:人白介素4(IL-4)以亚纳摩尔范围内的K_d与其细胞受体结合,类似于许多其他与造血素(细胞因子)受体超家族成员相互作用的4-螺旋束蛋白。在IL-4系统中,这种相互作用主要取决于受体链的胞外域(IL4-BP)(K_d≈150 pM)。现在,高分辨率的突变和动力学分析表明,IL-4的高亲和力结合来自位于螺旋A和C上的几个极性或带电氨基酸侧链的连续补片。

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