VE-L1序列分析及三维结构建模

Sequence analysis and three-dimensional structure modeling of VE-L1

目的:进一步研究血管内皮钙黏着素家族中成员VE-L1的结构及功能。方法:联合运用多种方法预测VE-L1的亲水性及其二级结构,利用同源建模法建构VE-L1的三维结构模型,在NCB I数据库中进行BLAST并构建同源进化树,在Scan Prosite数据库中进行Motif预测,对VE-L1进行序列分析并进行三维结构建模。结果:该蛋白为α+β结构的亲水性蛋白,预测其与VE-cadherin包含5个由约110个氨基酸重复区域组成(EC1-EC5)的结构一致,且与VE-cadherin在进化上具有较近的亲缘关系。结论:所预测的三维结构基本能反映出VE-L1真实的空间构象,为今后进一步理解和掌握VE-L1结构及功能的关系提供理论依据。

Objective： To make a sequence analysis and a three-dimensional structure modeling of VE L1. Methods： Various methods were used to predict a secondary structure, tertiary structure, phylogenetic tree of similar sequences and hydrophilicity of VE L1. Results ： A predicted secondary structure characteristic of α ＋ β protein was shown. By computation, VE L1 contains 5 conservative cadherin domains. The results showed that VE L1 had sequence homologu to VE cadherin. Conclusion： Three-dimensional structure modeling of VE L1 can be useful for mastering its structure and function.