The disulfide bond arrangement in the extracellular domain of the activin type II receptor.
The disulfide bond arrangement in the extracellular domain of the activin type II receptor.
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激活素 II 型受体胞外结构域中的二硫键排列。
DOI：
10.1023/a:1020640725959
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发表时间：
1999
期刊：
影响因子：
--
通讯作者：
Vale,W
中科院分区：
文献类型：
--
作者：
Fischer,WH;Greenwald,J;Park,M;Craig,AG;Choe,S;Vale,W
生长因子激活素的信号级联中的初始步骤涉及其与激活素II型受体的细胞外结构域的结合。该受体结构域含有10个半胱氨酸残基，其参与分子内二硫键。为了阐明该结构域的结构框架，我们已经使用高亲和力结合激活素A的受体的细胞外片段表征了其二硫键结合模式。通过将蛋白水解与质谱和化学序列分析相结合，确定二硫键连接如下：C1-C3、C2-C4、C5-C8、C6-C7和C9-C10。类似的二硫键排列出现在一个已知三维结构的蛇毒素家族中。
The initial step in the signaling cascade of the growth factor activin involves its binding to the extracellular domain of the activin type II receptor. This receptor domain contains 10 cysteine residues which are engaged in intramolecular disulfide bonds. To elucidate the structural framework of this domain we have characterized its disulfide-bonding pattern using an extracellular fragment of the receptor which binds activin A with high affinity. By combining proteolysis with mass spectroscopy and chemical sequence analysis, the disulfide connectivity was determined to be as follows: C1–C3, C2–C4, C5–C8, C6–C7, and C9–C10. A similar disulfide arrangement occurs in a family of snake toxins for which the three-dimensional structure is known.