• 作者： 劉宣良、林進中、何意、謝偉強、陳錦文、蘇永成
• 作者服務機構： Department of Chemical Engineering and Graduate Institute of Biotechnology, National Taipei University of Technology, Taipei 10608, Taiwan, R.O.C.
• 中文摘要： In this study, two structural models (denoted as MproST and MproSH) of the main proteinase (Mpro) from the novel coronavirus associated with severe acute respiratory syndrome (SARS-CoV) were constructed based on the crystallographic structures of Mpro from transmissible gastroenteritis coronavirus (TGEV) (MproT) and human coronavirus HcoV-229E (MproH), respectively. Various 200 ps molecular dynamics simulations were subsequently performed to investigate the dynamics behaviors of several structural features. Both MproST and MproSH exhibit similar folds as their respective template proteins. These structural models reveal three distinct functional domains as well as an intervening loop connecting domains II and III as found in both template proteins. In addition, domain III of these structures exhibits the least secondary structural conservation. A catalytic cleft containing the substrate binding subsites S1 and the S2 between domains I and II are also observed in these structural models. Although these structures share many common features, the most significant difference occurs at the S2 subsite, where the amino acid residues lining up this subsite are least conserved. It may be a critical challenge for designing anti-SARS drugs by simply screening the known database of proteinase inhibitors.
• 英文摘要： --
• 中文關鍵字： Main proteinase; Coronavirus; Severe acute respiratory syndrome (SARS); Molecular dynamics simulations; Functional domain; Structural model; Inhibitor.
• 英文關鍵字： --