Selected article for: "amino acid and SARS structure"
Author: Hong Zhou; Xing Chen; Tao Hu; Juan Li; Hao Song; Yanran Liu; Peihan Wang; Di Liu; Jing Yang; Edward C. Holmes; Alice C. Hughes; Yuhai Bi; Weifeng Shi
Title: A novel bat coronavirus reveals natural insertions at the S1/S2 cleavage site of the Spike protein and a possible recombinant origin of HCoV-19
  • Document date: 2020_3_5
    • ID: dbowa5bt_8
    Snippet: whereas the pangolin beta-CoV from Guangdong had amino acid identity of 97.4% 7 , and was 118 the closest relative of HCoV-19 in this region. A similarity plot estimated using Simplot 10 also 119 revealed that RmYN02 was more similar to HCoV-19 than RaTG13 in most genome regions 120 (Fig. 1b) . Again, in the RBD, the pangolin/MP789/2019 virus shared the highest sequence 121 identity to HCoV-19 (Fig. 1c) . 122 123 Results from both homology modell.....
    Document: whereas the pangolin beta-CoV from Guangdong had amino acid identity of 97.4% 7 , and was 118 the closest relative of HCoV-19 in this region. A similarity plot estimated using Simplot 10 also 119 revealed that RmYN02 was more similar to HCoV-19 than RaTG13 in most genome regions 120 (Fig. 1b) . Again, in the RBD, the pangolin/MP789/2019 virus shared the highest sequence 121 identity to HCoV-19 (Fig. 1c) . 122 123 Results from both homology modelling 1 , in vitro assays 2 and resolved three-dimensional 124 structure of the S protein 11 have revealed that like SARS-CoV, HCoV-19 could also use ACE2 125 as a cell receptor. We analyzed the RBD of RmYN02, RaTG13, and the two pangolin beta-126 CoVs using homology modelling (Fig. 2a-2f and Extended Data Figure 4 for sequence 127 author/funder. All rights reserved. No reuse allowed without permission.

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