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. 2016 Dec 23;27(1):119–129. doi: 10.1038/cr.2016.152

Figure 3.

Figure 3

Models of the SARS-CoV S monomer and trimer bound with the receptor ACE2. (A) “Binding” of the receptor ACE2 (green) to one S monomer (pink) of the conformation 1 S trimer. The CTD1 is in the “down” conformation. (B) “Binding” of the receptor ACE2 (green) to the conformation 1 S trimer. Three CTD1s are all in the “down” conformations. The steric clashes between a neighboring CTD1 (grey) and ACE2 (green) are colored blue. (C) The same model as in A, with the S trimer density map presented. Only the boundary profile of the “bound” ACE2 is shown (green lines) for a better view of the clashes (volume: 10 696 Å3). (D) “Binding” of the receptor ACE2 (green) with the conformation 3 S monomer (pink) of which the CTD1 is in the “up” conformation. (E) “Binding” of the receptor ACE2 (green) to the “up” CTD1 (pink) of the conformation 3 S trimer showing no steric clashes with any neighboring “down” CTD1 (grey). (F) The same model as in D with the S trimer 3D density map presented. All models are generated by superimposing the CTD1-ACE2 complex crystal structure onto the CTD1 of the corresponding SARS-CoV S monomer or trimer. The NTD models are not shown.