The solution structure of clip domains from Manduca sexta prophenoloxidase activating proteinase-2
The solution structure of clip domains from Manduca sexta prophenoloxidase activating proteinase-2
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DOI：
10.1021/bi7010724
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发表时间：
2007-10-16
期刊：
影响因子：
2.9
通讯作者：
Jiang, Haobo
中科院分区：
文献类型：
--
作者：
Huang, Rudan;Lu, Zhiqiang;Jiang, Haobo
剪辑结构域是节肢动物丝氨酸蛋白酶和一些蛋白水解无活性同系物中发现的结构模块，介导发育和免疫的细胞外信号通路。虽然对其结构或功能知之甚少，但剪辑域被认为是蛋白酶与其激活剂、辅因子和底物相互作用的位点。在这里，我们报道了来自 Manduca sexta 酚氧化酶激活蛋白酶 2 的双夹结构域的溶液结构。每个结构域均采用新的混合α/β折叠（两侧为两个α螺旋的三链反平行β折叠），并且该结构首次提供了来自催化活性蛋白酶的剪辑结构域的结构信息。对结构的检查结合来自不同组的夹结构域的多序列比对表明了底物结合位点、细菌相互作用区域和特定相互作用的表面。总之，我们的结果提供了对裁剪域函数的结构基础的见解，并且该结构可能代表了第 2 组裁剪域的原型。
Clip domains are structural modules found in arthropod serine proteinases and some proteolytically inactive homologues, which mediate extracellular signaling pathways of development and immunity. While little is known about their structures or functions, clip domains are proposed to be sites for interactions of proteinases with their activators, cofactors, and substrates. Here we report the solution structure of dual clip domains from Manduca sexta prophenoloxidase activating proteinase-2. Each domain adopts a new mixed alpha/beta fold (a three-stranded antiparallel beta-sheet flanked by two alpha-helices), and the architecture provides structural information on clip domains from a catalytically active proteinase for the first time. Examination of the structure in conjunction with a multiple sequence alignment of the clip domains from different groups suggests a substrate-binding site, a bacteria-interacting region, and a surface for specific interactions. In summary, our results provide insights into the structural basis of clip domain functions and this structure may represent the prototype of group-2 clip domains.