Three-dimensional model of the honeybee venom allergen Api m 7: structural and functional insights
Three-dimensional model of the honeybee venom allergen Api m 7: structural and functional insights
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DOI：
10.1039/b923127g
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发表时间：
2010-01-01
影响因子：
--
通讯作者：
Betzel, Christian
中科院分区：
文献类型：
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作者：
Georgieva, Dessislava;Greunke, Kerstin;Betzel, Christian
API m 7是蜂毒中主要的蛋白酶过敏原之一。它由丝氨酸蛋白酶样（SPL）和CUB结构域组成。关于API m 7的结构和功能的知识主要限于其氨基酸序列。使用它们的氨基酸序列和晶体学坐标的酚氧化酶原激活因子（PPAF-Ⅱ）作为模板的SPL域和坐标的猪精子黏附素PSP-II的CUB域的两个结构域的三维模型构建。API m 7的结构组织表明CUB结构域参与与天然底物的相互作用，而SPL结构域可能激活酶原。预测IgE抗原表位和抗原位点。API m 7显示出与PPAF-II家族成员的结构和功能相似性。本文对该酶可能的底物、功能和进化进行了讨论。
Api m 7 is one of the major protease allergens of the honeybee venom. It consists of a serine protease-like (SPL) and a CUB domain. The knowledge about the structure and function of Api m 7 is limited mainly to its amino acid sequence. Three-dimensional models of the two structural domains were constructed using their amino acid sequences and the crystallographic coordinates of prophenoloxidase-activating factor (PPAF-II) as a template for the SPL domain and the coordinates of porcine spermadhesin PSP-II for the CUB domain. The structural organization of Api m 7 suggests that the CUB domain is involved in interactions with natural substrates while the SPL domain probably activates zymogens. IgE epitopes and antigenic sites were predicted. Api m 7 shows structural and functional similarity to the members of the PPAF-II family. Possible substrates, function and evolution of the enzyme are discussed in the paper.