Author: Yuan, Yuan; Cao, Duanfang; Zhang, Yanfang; Ma, Jun; Qi, Jianxun; Wang, Qihui; Lu, Guangwen; Wu, Ying; Yan, Jinghua; Shi, Yi; Zhang, Xinzheng; Gao, George F.
Title: Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains Document date: 2017_4_10
ID: 094lgjnn_18
Snippet: Here we show that both MERS-CoV and SARS-CoV S trimers have flexible RBD, and then we further constructed the receptor binding models for the MERS-CoV or SARS-CoV S trimers by superimposition of the S trimer structures with the RBD-receptor complex structures through the RBD domain (Fig. 5) . We hypothesis that on the cell surface one CD26 may crosslink two S trimers by binding to standing RBDs, one from each trimer, whereas the monomeric ACE2 re.....
Document: Here we show that both MERS-CoV and SARS-CoV S trimers have flexible RBD, and then we further constructed the receptor binding models for the MERS-CoV or SARS-CoV S trimers by superimposition of the S trimer structures with the RBD-receptor complex structures through the RBD domain (Fig. 5) . We hypothesis that on the cell surface one CD26 may crosslink two S trimers by binding to standing RBDs, one from each trimer, whereas the monomeric ACE2 receptor will bind to the SARS-CoV S trimer in the pattern of one receptor to one S trimer (Fig. 5) . Thus, MERS-CoV might have higher avidity to receptor binding than SARS-CoV, when these two CoVs are attached to the host cell surface.
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