@article{APS9148,
author = {Xu Shen and Jian-Hua Xue and Chang-Ying Yu and Hai-Bin Luo and Lei Qin and Xiao-Jing Yu and Jing Chen and Li-Li Chen and Bin Xiong and Li-Duo Yue and Jian-Hua Cai and Jian-Hua Shen and Xiao-Min Luo and Kai-Xian Chen and Tei-Liu Shi and Yi-Xue Li and Geng-Xi Hu and Hua-Liang Jiang},
title = {Small envelope protein E of SARS: cloning, expression, purification, CD determination, and bioinformatics analysis.},
journal = {Acta Pharmacologica Sinica},
volume = {24},
number = {6},
year = {2016},
keywords = {},
abstract = {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.},
issn = {1745-7254}, url = {http://www.chinaphar.com/article/view/9148}
}