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紫花苜蓿蛋白质二硫键异构酶mPDI的生物信息学分析与同源建模 被引量:18

Bioinformatics Analysis and Homology Modeling Study of Protein Disulfide Isomerase (mPDI) from Medicago sativa L.
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摘要 紫花苜蓿蛋白质二硫键异构酶的基因已经被克隆测序。利用其mRNA及氨基酸序列,应用生物信息学软件预测了该蛋白质的理化性质、亲/疏水性、信号肽、二级结构、卷曲螺旋结构、跨膜区域、糖基化位点、活性位点、亚细胞定位、功能结构域及高级结构。结果表明,该蛋白质是一个整体疏水性蛋白,细胞定位为粗面内质网,含有512个氨基酸,理论等电点为4.98,信号肽位于1~24号氨基酸;二级结构中α-螺旋占26.37%(135AA),无规则卷曲占53.32%(273AA),延伸链占20.31%(104AA);包含3个卷曲螺旋结构,3个糖基化位点,2个硫氧还蛋白结构域,2个硫氧还蛋白活性位点。Ramachandram结构检测表明此模型的三维结构符合立体化学能量规则。 pai gene from Medicago soctiva L. encoding Protein Disulfide Isomerase(mPDI) has been cloned and sequenced. According to the mRNA and amino acid sequence, the character of mPDI such as the physical and chemical properties, hydrophilicity/hydrophobicity, signal peptide, secondary structure, coiled coil, transmembrane domains, O-glycogylation site, active site, subeellular localization, functional structural domains and three-dimensional structure were analyzed by a series of bioinformaties software. The results showed that mPDI was a hydrophobic and stable protein with 3 coiled coils, 30-glycogylation sites, 2 structural domains of thioredoxin, 2 active sites of thioredoxin, and located in rough endoplasmic retieulum. It has 512 amino acids, the theoretical pI is 4.98, and signal peptide located in 1-24AA. In the sec-ndary structure, α-helix, random coil, extended chain is 26.37% , 53.32% , 20.31% respectively. The validation of modeling accords with the stereochemistry.
出处 《安徽农业科学》 CAS 北大核心 2009年第33期16263-16267,16288,共6页 Journal of Anhui Agricultural Sciences
基金 曲靖师范学院校内青年科研基金项目(2008QN031)
关键词 紫花苜蓿 蛋白质二硫键异构酶 同源建模 Medicago sativa L. Protein disulfide isomerase Homology modeling
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