牡蛎过敏原Crag1蛋白的结构分析

Structural Analysis of Crag1 Protein from Oyster Allergens

通过生物信息学方法,分析牡蛎过敏原Crag1蛋白的理化性质和各级结构。结果显示,牡蛎Crag1蛋白由284个氨基酸组成,其酸性氨基酸和亲水性氨基酸较多; Crag1蛋白氨基酸序列与角蝾螺、九孔螺原肌球蛋白(Tropomyosin, Tm)的同源性较高,亲缘关系较近,亲疏水性区域相似; DNA Star分析可知α-螺旋是Crag1蛋白二级结构的主要部分; Swiss-Model建模的结果表明,模拟形成的Crag1三维构象有较高的稳定性和合理性,且空间结构比较简单,没有复杂的三四级结构;此次试验为研究牡蛎Crag1蛋白结构和过敏性的关系及不同物种过敏原间的交叉反应提供了理论依据。

Through bioinformatics methods, the physicochemical properties and various structures of Crag1 protein from oyster allergens were analyzed. The results showed that Crag1 protein was composed of 284 amino acids, with more acidic amino acids and hydrophilic amino acids. The amino acid sequence of Crag1 protein was highly homologous to ocellata and porphosporins. Their phylogenetic relationship was relatively close and the hydrophilic and hydrophobic regions were similar. DNA Star analysis showed that α-helix was the main part of the secondary structure of Crag1 protein;Swiss-Model modeling results showed that the Crag1 3D conformation formed by simulation had higher stability and rationality, and the spatial structure was relatively simple. There was no complicated tertiary or quaternary structure;A theoretical basis for studying the structure and allergic relationship of Crag1 protein in oysters and cross reaction between allergens of different species was provided.