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. 2008 Apr 30;82(14):6984–6991. doi: 10.1128/JVI.00442-08

FIG. 4.

FIG. 4.

Structural basis for host adaptations of residue 487 on SARS-CoV RBD. (A) On the surface of unbound human ACE2 (28), Lys353 points into solution. (B) At the interface of human ACE2 and hTor02 (11), Lys353 on ACE2 is embedded in a hydrophobic tunnel surrounded by Thr487 on hTor02 RBD and three tyrosines. Lys353 and Asp38 on ACE2 form a salt bridge, which requires support from RBD Thr487. (C) At the interface of chimeric ACE2 and hTor02, Glu38 and Lys353 on ACE2 form a bifurcated salt bridge, in the presence of RBD Thr487. (D) At the interface of chimeric ACE2 and cGd05, Glu38 and Lys353 on ACE2 form a strong bifurcated salt bridge, in the presence of RBD Ser487. (E) Electron density map of the interface of chimeric ACE2 and cGd05, as part of a composite-omit map calculated from the refined model of chimeric ACE2 complexed with cGd05 RBD. (F) Corey-Pauling-Koltun presentation of the hydrophobic tunnel surrounding ACE2 Lys353 at the interface of chimeric ACE2 and cGd05. The illustrations were made using Povscript (4).