中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Small envelope protein E of SARS: cloning, expression, purification, CD determination, and bioinformatics analysis

文献类型:期刊论文

作者Shen, X; Xue, JH; Yu, CY; Luo, HB; Qin, L; Yu, XJ; Chen, J; Chen, LL; Xiong, B; Yue, LD
刊名ACTA PHARMACOLOGICA SINICA
出版日期2003-06
卷号24期号:6页码:505-511
关键词severe acute respiratory syndrome (SARS) small envelope protein gene expression bioinformatics circular dichroism spectroscopy
ISSN号1671-4083
文献子类Article
英文摘要AIM: To obtain the pure sample of SARS small envelope E protein (SARS E protein), study its properties and analyze its possible functions. METHODS: The plasmid of SARS E protein was constructed by the polymerase chain reaction (PCR), and the protein was expressed in the E coli strain. The secondary structure feature of the protein was determined by circular dichroism (CD) technique. The possible functions of this protein were annotated by bioinformatics methods, and its possible three-dimensional model was constructed by molecular modeling. RESULTS: The pure sample of SARS E protein was obtained. The secondary structure feature derived from CD determination is similar to that from the secondary structure prediction. Bioinformatics analysis indicated that the key residues of SARS E protein were much conserved compared to the E proteins of other coronaviruses. In particular, the primary amino acid sequence of SARS E protein is much more similar to that of murine hepatitis virus (MHV) and other mammal coronaviruses. The transmembrane (TM) segment of the SARS E protein is relatively more conserved in the whole protein than other regions. CONCLUSION: The success of expressing the SARS E protein is a good starting point for investigating the structure and functions of this protein and SARS coronavirus itself as well. The SARS E protein may fold in water solution in a similar way as it in membrane-water mixed environment. It is possible that beta-sheet I of the SARS E protein interacts with the membrane surface via hydrogen bonding, this beta-sheet may uncoil to a random structure in water solution.
WOS关键词MURINE CORONAVIRUS ; MEMBRANE-PROTEIN ; VIRUS ; PARTICLES
WOS研究方向Chemistry ; Pharmacology & Pharmacy
语种英语
CSCD记录号CSCD:1273714
WOS记录号WOS:000183575100004
出版者SHANGHAI INST MATERIA MEDICA
源URL[http://119.78.100.183/handle/2S10ELR8/274226]  
专题新药研究国家重点实验室
中科院受体结构与功能重点实验室
通讯作者Shen, X
作者单位1.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai Inst Biol Sci, State Key Lab Drug Res,Drug Discovery & Design Ct, Shanghai 201203, Peoples R China
2.Shanghai Hlth Digit Ltd, Shanghai 200233, Peoples R China
3.Shanghai Ctr Bioinformat Technol, Shanghai 201203, Peoples R China
4.Chinese Acad Sci, Shanghai Inst Biol Sci, Bioinformat Ctr, Shanghai 200031, Peoples R China
5.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, Shanghai 200031, Peoples R China
推荐引用方式
GB/T 7714
Shen, X,Xue, JH,Yu, CY,et al. Small envelope protein E of SARS: cloning, expression, purification, CD determination, and bioinformatics analysis[J]. ACTA PHARMACOLOGICA SINICA,2003,24(6):505-511.
APA Shen, X.,Xue, JH.,Yu, CY.,Luo, HB.,Qin, L.,...&Jiang, HL.(2003).Small envelope protein E of SARS: cloning, expression, purification, CD determination, and bioinformatics analysis.ACTA PHARMACOLOGICA SINICA,24(6),505-511.
MLA Shen, X,et al."Small envelope protein E of SARS: cloning, expression, purification, CD determination, and bioinformatics analysis".ACTA PHARMACOLOGICA SINICA 24.6(2003):505-511.

入库方式: OAI收割

来源:上海药物研究所

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