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首页> 外文期刊>Journal of Molecular Biology >Mutational analysis and NMR studies of the death domain of the tumor necrosis factor receptor-1.
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Mutational analysis and NMR studies of the death domain of the tumor necrosis factor receptor-1.

机译：肿瘤坏死因子受体-1死亡域的突变分析和NMR研究。

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摘要

Tumor necrosis factor receptor-1 (TNFR-1) death domain (DD) is the intracellular functional domain responsible for the receptor signaling activities. To understand the transduction mechanism of TNFR-1 signaling we performed structural and functional analysis of the TNFR-DD. The secondary structure of the TNFR-DD shows that it consists of six anti-parallel alpha-helices. The determination of the topological fold and an extensive mutagenesis analysis revealed that there are two opposite faces that are involved in self-association and interaction with the TRADD death domain. Interestingly, the same critical residues in TNFR-DD are involved in both interactions. There is a good correlation between the binding activities of the mutant proteins and their cytotoxic activities. These results provide important insight into the molecular interactions mediating TNFR-DD self-association and subsequent recruitment of TRADD in the signaling activity of TNFR-1. Copyright 2000 Academic Press.
机译：肿瘤坏死因子受体1（TNFR-1）死亡域（DD）是负责受体信号传导活性的细胞内功能域。为了理解TNFR-1信号转导的机制，我们进行了TNFR-DD的结构和功能分析。 TNFR-DD的二级结构表明它由六个反平行的α螺旋组成。拓扑倍数的确定和广泛的诱变分析表明，有两个相对的面孔参与自我关联以及与TRADD死亡域的相互作用。有趣的是，TNFR-DD中相同的关键残基参与了两种相互作用。突变蛋白的结合活性与其细胞毒性活性之间具有良好的相关性。这些结果为介导TNFR-DD自缔合的分子相互作用以及随后TRADD在TNFR-1信号传导活性中的募集提供了重要的见识。版权所有2000学术出版社。

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