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首页> 外文期刊>The biochemical journal >Functional analysis of tumour necrosis factor-α-related apoptosis-inducing ligand (TRAIL): cysteine-230 plays a critical role in the homotrimerization and biological activity of this novel tumoricidal cytokine
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Functional analysis of tumour necrosis factor-α-related apoptosis-inducing ligand (TRAIL): cysteine-230 plays a critical role in the homotrimerization and biological activity of this novel tumoricidal cytokine

机译:肿瘤坏死因子-α相关细胞凋亡诱导配体的功能分析(踪迹):半胱氨酸-230在这种新的肿瘤细胞因子的同型肿瘤和生物活性中起着关键作用

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pWe have determined that the mutation of the cysteine-230 residue to either glycine or serine in TRAIL (tumour necrosis factor-α-related apoptosis-inducing ligand) results in the formation of a structurally incompetent dimer and a consequent loss of apoptotic activity. Similarly, chemical modification of the thiol residues present in both reduced and Znsup2+/sup-depleted trimer converts TRAIL into an inactive dimer. We postulate that cysteine-230 plays a critical role in homotrimerization of this tumoricidal cytokine./p
机译:我们已经确定半胱氨酸-230残基的突变到甘氨酸或血清中的甘氨酸(肿瘤坏死因子-α相关的凋亡诱导配体)导致形成结构不称解的二聚体和随之而来的凋亡丧失活动。类似地,在还原和Zn 2 + 2 + 2 + 2 + 2 + -depleted三聚体中的硫醇残基的化学改性将痕迹转化为无活性二聚体。我们假设半胱氨酸-230在这种肿瘤细胞因子的同态化中起着关键作用。

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