四川动物
四川動物
사천동물
SICHUAN JOURNAL OF ZOOLOGY
2008年
6期
997-1002
,共6页
SOX蛋白%MATLAB%同源建模%三级结构%东北虎
SOX蛋白%MATLAB%同源建模%三級結構%東北虎
SOX단백%MATLAB%동원건모%삼급결구%동북호
Sox protein%MATLAB%homology modeling%tertiary structure%Panthera tigris altaica
SOX蛋白具有一个与DNA特异结合的高保守HMG-box结构域.为研究东北虎SOX蛋白三级结构的分子机理,利用MATLAB的Bioinfonnatics工具从GenBank中下载东北虎SOX蛋白序列信息,以三级结构已知的SOX2为模板,联合SwissPdbViewer与MATLAB,采用同源建模方法对SOX蛋白HMG-box进行建模、预测;利用MATLAB的Visualization Tool分析预测结果的三维结构.结果显示PtSox蛋白的HMG-box由3个α-螺旋和2个loop区构成;热稳定性分析表明PtSox蛋白loop区的热力学结构不稳定;表面静电分布显示出PtSox蛋白C-端的中间有一个可能与其它小分子或蛋白质的相互作用位点的N/C腔,上述空间结构可能与其活性与功能的调控有关.
SOX蛋白具有一箇與DNA特異結閤的高保守HMG-box結構域.為研究東北虎SOX蛋白三級結構的分子機理,利用MATLAB的Bioinfonnatics工具從GenBank中下載東北虎SOX蛋白序列信息,以三級結構已知的SOX2為模闆,聯閤SwissPdbViewer與MATLAB,採用同源建模方法對SOX蛋白HMG-box進行建模、預測;利用MATLAB的Visualization Tool分析預測結果的三維結構.結果顯示PtSox蛋白的HMG-box由3箇α-螺鏇和2箇loop區構成;熱穩定性分析錶明PtSox蛋白loop區的熱力學結構不穩定;錶麵靜電分佈顯示齣PtSox蛋白C-耑的中間有一箇可能與其它小分子或蛋白質的相互作用位點的N/C腔,上述空間結構可能與其活性與功能的調控有關.
SOX단백구유일개여DNA특이결합적고보수HMG-box결구역.위연구동북호SOX단백삼급결구적분자궤리,이용MATLAB적Bioinfonnatics공구종GenBank중하재동북호SOX단백서렬신식,이삼급결구이지적SOX2위모판,연합SwissPdbViewer여MATLAB,채용동원건모방법대SOX단백HMG-box진행건모、예측;이용MATLAB적Visualization Tool분석예측결과적삼유결구.결과현시PtSox단백적HMG-box유3개α-라선화2개loop구구성;열은정성분석표명PtSox단백loop구적열역학결구불은정;표면정전분포현시출PtSox단백C-단적중간유일개가능여기타소분자혹단백질적상호작용위점적N/C강,상술공간결구가능여기활성여공능적조공유관.
Sox proteins are characterized by a conserved hiigh mobility group HMG-box domain,which is responsible for DNA binding andbonding.In order to research the molecular mechanism of Sox protein in Panthera tigris altaica,the amino acid sequences of PtSox were downloaded from the C,enBank database using bioinformatics tools of MATLAB.The tertiary structures of PtSox proteins were modeled using computer programs SwissPdbViewer and MATLAB,homology modeling method,and the known tertiary structure of Sox2 as templates.The three-dimensional structures of predicted PtSox proteins were visualized using Visualization Tool of MATLAB.The results showed that the tertiary structure of PtSox appeared to three α-helices and two loop regions.Thermestability analysis showed that the loop regions of PtSox structures were relatively unstable thermodynamically.Analysis of the electrostatic surfaces showed the C-terminal half of PtSox formed an N/C cavity where interacted with organic molecules or proteins could be possible.This observation suggested that the spatial structure of Sox was more likely to regulate the activity and function of this protein.