徐国强,胡晓霞,潘娅,董宇华,张金娟,张敏,张祥令,臧贵勇,熊英,王旭东,陈腾祥
XU Guoqiang1,HU Xiaoxia1,PAN Ya1,DONG Yuhua1,ZHANG Jinjuan2,ZHANG Min1,ZHANG Xiangling3,ZANG Guiyong4,XIONG Ying2,WANG Xudong1,CHEN Tengxiang1 (1.Department of Physiology

• 1:贵阳医学院生理学教研室
• 2:贵阳医学院机能实验室
• 3:贵阳医学院组织胚胎学教研室
• 4:贵阳医学院解剖学教研室

摘要(Abstract)：

目的:对人钙激活中性蛋白酶(calpain)的2个亚家族成员calpain-1和calpain-2进行功能的比较分析。方法:以美国生物技术国家中心(NCBI)的蛋白质数据库获取人calpain-1和calpain-2的参考序列号(Ref-Seq)和氨基酸序列,通过UniProt数据库检索2个蛋白的一般蛋白质功能注释,获取相关结构域信息;利用DNA-MAN软件对结构域进行序列比对,用蛋白质结构数据(PBD)和蛋白修饰数据库(PhosphoSit Plus)进行修饰位点空间分布的分析及用String9.0软件进行蛋白质-蛋白质相互作用分析。结果:结构域比对分析显示,人calpain-1和calpain-2的钙蛋白酶催化结构域保守性程度高,而EF-hand结构域的差异比较大;翻译修饰分析发现,2个蛋白的修饰有明显的不同,人calpain-1的修饰比较单一,仅发现在赖氨酸(K84)有乙酰化修饰,而calpain-2的修饰形式和位点相对多样,分布在分子表面、间隙内及分子内部。相互作用分析发现,与人calpain-1和calpain-2相互作用的蛋白质有少部分是相同的,而多数是不同的,分别与不同细胞活动有关。结论:人calpain-1和cal-pain-2的钙蛋白酶催化结构域是高度保守的,二者功能上差异主要是由于调控位点(EH-hand和翻译后修饰位点)的差异引起。
Objective:To compare the function of human calpain-1 and calpain-2,two classic sub-family proteins of calcium-activated neutral protease.Methods:The RefSeq and amino acid sequences of human calpain-1 and-2 were acquired from the protein database of American national center for biotechnology(NCBI).The general protein annotation and domain information of calpain-1 and-2 were obtained from UniProt database.DNAMAN software was used to compare the primary structure of domains of the two calpains,and the distribution of modified sites were detected with protein data bank(PBD) and protein modification database(PhosphoSit Plus)jointly.String 9.0 was used in the analysis of protein-protein interaction.Results:As analysis of domain showing,calpain catalytic domain of the two calpains were highly conserved,while the variation in EF-hand domain was relatively large.The post-translational modification(PTM) in calpain-1 was only on lys(K)84,while in calpain-2 was more complex which could be found on the surface,in the cleft and inside the molecular in different forms.The protein-protein interaction analysis indicated that there were only few proteins commonly in both interaction maps,while most proteins were specific in individual maps of the two calpains,which associated with different cell activities.Conclusion:The catalytic domains of human calpain-1 and calpain-2 are highly conserved.The functional differences between them are mainly caused by the alteration of regulating sites(EF-hand domain and PTM sites).

关键词(KeyWords)： 钙激活中性蛋白酶;催化亚基;生物信息学;结构域;翻译后修饰
calcium-activated neutral protease;catalytic subunit;bioinformatics;domain;post-translational modification

Abstract:

Keywords:

基金项目(Foundation): 国家自然科学基金资助项目:NO.81060176;; 贵州省科技厅自然基金项目:黔科合J字[2008]2280

作者(Author): 徐国强,胡晓霞,潘娅,董宇华,张金娟,张敏,张祥令,臧贵勇,熊英,王旭东,陈腾祥
XU Guoqiang1,HU Xiaoxia1,PAN Ya1,DONG Yuhua1,ZHANG Jinjuan2,ZHANG Min1,ZHANG Xiangling3,ZANG Guiyong4,XIONG Ying2,WANG Xudong1,CHEN Tengxiang1 (1.Department of Physiology

DOI: 10.19367/j.cnki.1000-2707.2011.04.003

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