Extended Data Fig. 7: Analysis of RBD of the spike protein of WHCV coronavirus. | Nature

Extended Data Fig. 7: Analysis of RBD of the spike protein of WHCV coronavirus.

From: A new coronavirus associated with human respiratory disease in China

Extended Data Fig. 7

a, Amino acid sequence alignments of RBD sequences of SARS-like CoVs. Three bat SARS-like CoVs—which could efficiently use the human ACE2 as receptor—had an RBD sequence of similar size to SARS-CoV. WHCV contains a single Val470 insertion. The key amino acid residues involved in the interaction with human ACE2 are marked by orange squares. By contrast, five bat SARS-like CoVs, including Rp3, which has previously been found not to bind to ACE214—had amino acid deletions in two motifs (amino acids 433–437 and 460–472, highlighted by red boxes) compared with those of SARS-CoV.11 b, The two motifs (amino acids 433–437 and 460–472) are shown in red for the crystal structure of the RBD of the spike protein of SARS-CoV in complex with the human ACE2 receptor (PDB 2AJF). Human ACE2 is shown in blue and the RBD of the spike protein of SARS-CoV is shown in green. Important residues in human ACE2 that interact with the RBD of the spike protein of SARS-CoV are marked. c, Predicted protein structure of the RBD of the spike protein of WHCV based on target–template alignment using ProMod3 on the SWISS-MODEL server. d, Predicted structure of the RBD of the spike protein of SARS-like CoV Rs4874. e, Predicted structure of the RBD of the spike protein of SARS-like CoV Rp3. f, Crystal structure of the RBD of the spike protein of SARS-CoV (green) (PDB 2GHV). Motifs that resemble amino acids 433–437 and 460–472 of the spike protein of SARS-CoV are shown in red.

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