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

FIG. 3.

FIG. 3.

Structural basis for host adaptations of residue 479 on SARS-CoV RBD. (A) On the surface of unbound human ACE2 (28), Lys31 points into solution. (B) At the interface of human ACE2 and hTor02 (11), Lys31 on ACE2 folds back and forms a salt bridge with Glu35 on ACE2. Asn479 on RBD forms hydrophobic interactions with Tyr440 and Tyr442 on RBD. (C) At the interface of chimeric ACE2 and hTor02, Thr31 cannot form a salt bridge with Glu35 on civet ACE2. Consequently, Glu35 on civet ACE2 is unneutralized. (D) At the interface of chimeric ACE2 and cSz02, Lys479 on RBD forms a salt bridge with Glu35 on civet ACE2 and hydrophobic interactions with tyrosines. (E) At the interface of chimeric ACE2 and cGd05, Arg479 on RBD forms a strong bifurcated salt bridge with Glu35 on civet ACE2 and strong hydrophobic interactions with tyrosines. (F) 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. The illustrations were made using Povscript (4).