Structure exploration and function prediction of SARS coronavirus E protein

SARS E protein has long been taken only as membrane component of coronavirus. However, the researches have revealed that E proteins play an important multifunctional role in coronavirus virion life cycle. This investigation aims at exploring the three-dimensional (3D) structure of SARS E protein, especially for the loop region of its functional potential. As a result, a possible active site is found to be a cleavage in the C terminal, which is made up of nine amino acids. Additionally, the electrostatic property was employed to conform the possible active site. Electrostatic potential analysis prove that the active site really possesses the largest electrostatic property among the whole molecule domain, accordingly it will have a larger charge deposition and therefore may have stronger capabilities of interaction with possible ligand as well as other protein. The simulation results are helpful to providing insights into understanding the functions of SARS E protein and establishing molecular models for screening anti-SARS drug design.