Crystal structure of RVV‐X: An example of evolutionary gain of specificity by ADAM proteinases
Crystal structure of RVV‐X: An example of evolutionary gain of specificity by ADAM proteinases
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DOI：
10.1016/j.febslet.2007.11.062
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发表时间：
2007-12
期刊：
影响因子：
3.5
通讯作者：
S. Takeda;T. Igarashi;H. Mori
中科院分区：
文献类型：
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作者：
S. Takeda;T. Igarashi;H. Mori
罗素蛇毒因子X激活剂（RVV-X）是一种异三聚体金属蛋白酶，具有类似哺乳动物adam的重链和两条类似凝集素的轻链。RVV-X的晶体结构已在2.9Å分辨率下确定，并显示出钩子-扳手-扳手样结构，其中金属蛋白酶/解体素区域构成钩子，凝集素样结构域构成手柄。该结构为多亚基蛋白的分子进化提供了一个典型的例子，并深入了解了ADAM/adamalysin/ relysin蛋白酶对靶标识别和蛋白水解的分子基础。
Russell’s viper venom factor X activator (RVV-X) is a heterotrimeric metalloproteinase with a mammalian ADAM-like heavy chain and two lectin-like light chains. The crystal structure of RVV-X has been determined at 2.9Å resolution and shows a hook-spanner-wrench-like architecture, in which the metalloproteinase/disintegrin region constitutes a hook, and the lectin-like domains constitute a handle. A 6.5nm separation between the catalytic site and a putative exosite suggests a docking model for factor X. The structure provides a typical example of the molecular evolution of multi-subunit proteins and insights into the molecular basis of target recognition and proteolysis by ADAM/adamalysin/reprolysin proteinases.