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. 2019 Jun 6;8(1):841–856. doi: 10.1080/22221751.2019.1624482

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© 2019 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group, on behalf of Shanghai Shangyixun Cultural Communication Co., Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — Structural insights of the MERS-CoV spike glycoprotein. (A–B) Top and side view of the MERS-CoV spike trimer with all RBD in ‘down' position, shown as molecular surface (PDB ID: 5W9J). The three protomers are coloured green, lightblue, and red, respectively. The labels are the same with those in Figure 1. (C) One of the three protomers in (B) is highlighted as cartoon representation whereas the other two protomers are faded in white. The RBD in ‘down' position is coloured in green. The non-RBD S1 region was coloured deep blue and the S2 region was coloured orange. (D) Superimposition of RBD-bound DPP4 (PDB ID: 4L72) into the MERS-CoV spike trimer. Clashes were observed between DPP4 and the other two S1 regions in the trimer structure. (E–F) Top and side view of the MERS-CoV spike trimer with one RBD in ‘up' position and the other two in ‘down' position, shown as molecular surface (PDB ID: 5W9H). Same colour codes are used as in (A–B). (G) The protomer with RBD in ‘up' position is highlighted as cartoon representation, with RBD in green, non-RBD S1 region in deep blue, and S2 in orange. (H) Superimposition of the RBD-bound DPP4 into the MERS-CoV spike trimer, with DPP4 interacting with the ‘up' RBD. No steric clash was observed.