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哺乳动物乙酰胆碱酯酶的结构预测与选择压力检测    

Selection pressure analysis and protein structure prediction of mammal acetylcholinesterases

文献类型:期刊文献

中文题名:哺乳动物乙酰胆碱酯酶的结构预测与选择压力检测

英文题名:Selection pressure analysis and protein structure prediction of mammal acetylcholinesterases

作者:朱红霞[1];胡利宗[2,3];任敏[1];邓小莉[1]

第一作者:朱红霞

机构:[1]新乡学院生命科学与技术系;[2]中国科学院遗传发育研究所;[3]中国科学院研究生院

第一机构:新乡学院生命科学技术学院

年份:2012

卷号:39

期号:9

起止页码:133-136

中文期刊名:广东农业科学

外文期刊名:Guangdong Agricultural Sciences

收录:CSTPCD;;北大核心:【北大核心2011】;CSCD:【CSCD_E2011_2012】;

基金:河南省政府决策研究招标课题(B578)

语种:中文

中文关键词:哺乳动物;乙酰胆碱酯酶;选择压力;结构预测

外文关键词:mammal; acetylcholinesterases; selective pressure; protein structure prediction

摘要:乙酰胆碱酯酶(AChE)是一种丝氨酸水解酶,是哺乳动物神经传导中的关键性酶。为研究不同哺乳动物AChE基因在进化过程中是否发生了适应性进化,基于位点模型与分支位点模型对哺乳动物11条AChE蛋白序列所受到的选择压力进行了检测,并模建了绒猴的蛋白结构。结果表明:11个哺乳动物AChE蛋白中,几乎所有的分支和位点均处于强烈的负选择压力下;在所有分枝中,位点模型鉴定了1个共同的正选择位点Ala389;此外,分支位点模型鉴定了绒猴分支中的Tyr285和Glu392处于正选择压力,发生了适应性进化。最后,将3个正选择位点定位在绒猴AChE蛋白的立体结构中,为直观观察与分析蛋白适应性进化位点提供了便捷,为进一步功能分析AChE活性位点提供了线索。
Acetylcholinesterases (ACHE) were serine hydrolases that played an important role in mammal neutral transduction. In order to investigation of adaptive evolution in mammal acetylcholinesterases, site-specific model and branch-site model were used to detect selective pressures within 11 mammal AChE proteins. Additionally, the AChE protein in Callithrix jacchus was predicted using homologous model method. The results showed as follows: purifying selection controlled almost all the branches and sites in phylogenetic tree constructed by 11 mammal AChE proteins; Ala389, one positive selection site was identified using the site-specific model in all the branches in phylogenetic tree; moreover, Tyr285 and Glu392 displayed adaptive evolution along the only Callithrix jacchus branch from phylogenetic tree, however other branches remained purifying selection. Finally, mapping of Tyr285, Glu392, and Ala389 on the AChE protein in Callithrix jacchus allowed to visualization and investigation of adaptive evolution directly and easily. This study provides a useful clue for further functional study of active sites in AChE protein.

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