[1]许宏宣,刘小强,常凯.肿瘤相关Smads家族蛋白的计算机模拟修饰[J].西华师范大学学报(自然科学版),2018,39(04):383-389.[doi:10.16246/j.issn.1673-5072.2018.04.008]
 XU Hongxuan,LIU Xiaoqiang,CHANG Kai.Computer Simulated Modification of TumorAssociated Smads Family Protein[J].Journal of China West Normal University(Natural Sciences),2018,39(04):383-389.[doi:10.16246/j.issn.1673-5072.2018.04.008]
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肿瘤相关Smads家族蛋白的计算机模拟修饰

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《西华师范大学学报(自然科学版)》[ISSN:1673-5072/CN:51-1699/N]

卷:
39
期数:
2018年04期
页码:
383-389
栏目:
出版日期:
2018-12-20

文章信息/Info

Title:

Computer Simulated Modification of TumorAssociated Smads Family Protein

作者:

许宏宣12刘小强1常凯3

(1.西南大学 a生命科学学院,b西南大学-西藏农牧学院药用植物联合研发中心,重庆  400715;2.成都市实验外国语学校生物教研组,成都  611130;3.中国人民解放军成都军区总医院检验科,成都  610083;)

Author(s):

XU  Hongxuan12LIU  Xiaoqiang1CHANG  Kai3

(1.SWU-TAAHC Medicinal Plant Joint R&D Centre,School of Life Sciences,Southwest University,Chongqing 400715,China;2.Biology Teaching and Research Group,Chengdu Experiment Foreign Languages School,Chengdu Sichuan 611130,China;3.Department of Medical Laboratory,Chengdu Military General Hospital PLA,Chengdu Sichuan 610083,China)

关键词:

Smad蛋白信息学分析结构模拟蛋白修饰

Keywords:

Smad protein familybioinformation analysisstructural simulationprotein modification

分类号:
Q518.4
DOI:
10.16246/j.issn.1673-5072.2018.04.008
文献标志码:
A
摘要:

本文旨在比较分析Smad蛋白家族的结构与功能特性,进而对不稳定蛋白进行模拟修饰,为深入开展Smad蛋白功能研究奠定基础;应用生物信息学对比分析Smad蛋白质家族成员的理化特性、结构特点及功能差异,基于各自特征对不稳定蛋白质进行修饰预测并评估其稳定性;结果表明氨基酸序列的相似性在Smad亚家族内极高;亚家族间则较低。家族各成员分子量、等电点、消光系数等理化性质差异显著,各成员均为疏水性蛋白(GRAVY<0)且体外稳定性较差(Instability index>40)。测定Smad蛋白质的pI值和消光系数能够有效对Smad进行快速分类。比较分析亚家族间蛋白质结合位点和三维结构均具有与蛋白质的功能相对应的标志性特征,体现了各成员的功能多样性。最后就研究热点蛋白Smad4,6,7的不稳定结构进行模拟突变,预测蛋白质在体外环境15~50 ℃区间相对稳定;对Smad蛋白家族进行了系统的对比分析,并对不稳定蛋白进行了理想的模拟修饰,为进一步开展Smad在肿瘤发生途径与作用机制中的研究提供依据。

Abstract:

To lay a foundation for further research on the function of Smad protein,this paper analyzes the protein structure,functional characteristics of Smad protein family,modify and predict the unstable protein.The physicochemical properties,structural features and functional difference of Smad protein family are compariatively analyzed by Applied Bioinformatics.Based on its different characteristics, the modification of unstable protein is predicted and its stability is evaluated.The result shows that the similarity of the amino acid sequence is very high in Smad subfamily but very low in other subfamilies.Significant differences are found in the molecular weight,isoelectric point,extinction coefficient and other physical and chemical properties of each member of the family.All of the proteins are hydrophobic (GRAVY<0) but with poor stability in vitro(Instability index>40).The measured pI value and extinction coefficient of protein are efficient in classifying Smad in a quick way.The binding sites and 3D structures are consistent with the functional difference of proteins,reflecting the diversity of protein functions.The simulated mutation of unstable protein 4,6,7  are carried out to predict the stability of protein in an external enviroment of 15~50 ℃.The comparative analysis and ideal modification of Smad protein family can provide a basis for the further study of Smad in pathogenesis and mechanism of tumorigenesis.

备注/Memo

备注/Memo:

收稿日期:2018-06-08
作者简介:许宏宣(1987—),女,重庆梁平人,中学一级教师,主要从事生物技术与分子生物学研究与教学。
通信作者:常凯(1988—),男,四川成都人,主管技师,主要从事医学遗传学与分子诊断研究,E-mail:ck8148@126.com

更新日期/Last Update: 2018-12-20