Author: Chunyun Sun; Long Chen; Ji Yang; Chunxia Luo; Yanjing Zhang; Jing Li; Jiahui Yang; Jie Zhang; Liangzhi Xie
Title: SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development Document date: 2020_2_20
ID: nhq0oq8y_8
Snippet: The structure model for SARS-CoVRBD-ACE2 complex was optimized based on the complex's crystal structure (PDB ID: 2AJF) (http://www.rcsb.org/). The structure model for SARS-CoV-2 RBD-ACE2 complex was constructed by homology modeling using the optimized SARS-CoV RBD-ACE2 complex crystal structure as a template, based on a 73.7% amino acid sequence homology between the two viruses. Root-mean-square deviation (RMSD) of Cα atoms between the two compl.....
Document: The structure model for SARS-CoVRBD-ACE2 complex was optimized based on the complex's crystal structure (PDB ID: 2AJF) (http://www.rcsb.org/). The structure model for SARS-CoV-2 RBD-ACE2 complex was constructed by homology modeling using the optimized SARS-CoV RBD-ACE2 complex crystal structure as a template, based on a 73.7% amino acid sequence homology between the two viruses. Root-mean-square deviation (RMSD) of Cα atoms between the two complex structures is 0.703 Å, indicating an almost identical structural conformation (Figure1B). There are subtle differences in the RBD-ACE2 interfaces between SARS-CoV-2 and SARS-CoV at the loop 469-470 (numbered according to SARS-CoV RBD), arising from a one-residue insertion after residue 469 ( Figure 1A) .
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