Selected article for: "high percentage and RBD domain"
Author: Ivan Mercurio; Vincenzo Tragni; Francesco Busco; Anna De Grassi; Ciro Leonardo Pierri
Title: Protein structure analysis of the interactions between SARS-CoV-2 spike protein and the human ACE2 receptor: from conformational changes to novel neutralizing antibodies
  • Document date: 2020_4_18
    • ID: mswmkgl4_39
    Snippet: Thanks to the high percentage of identical residues (> 75 %) between SARS-CoV-1 and SARS-CoV-2 spike RBD domains and to their highly similar tertiary structure, as observed from the RMSD of 0.5 Ã… between the coordinates of RBDs from SARS-CoV-1 (6nb7.pdb, (45) and 2dd8.pdb, (44) ) and SARS-CoV-2 (6vw1.pdb (54) and 6vsb.pdb, (21)) spike proteins, it was possible to evaluate interactions between m396 and SARS-CoV-2 spike RBD and to propose a sequen.....
    Document: Thanks to the high percentage of identical residues (> 75 %) between SARS-CoV-1 and SARS-CoV-2 spike RBD domains and to their highly similar tertiary structure, as observed from the RMSD of 0.5 Ã… between the coordinates of RBDs from SARS-CoV-1 (6nb7.pdb, (45) and 2dd8.pdb, (44) ) and SARS-CoV-2 (6vw1.pdb (54) and 6vsb.pdb, (21)) spike proteins, it was possible to evaluate interactions between m396 and SARS-CoV-2 spike RBD and to propose a sequence/structure of an ideal FAB m396-based chimeric antibody for targeting SARS-CoV-2 spike RBD domain, preventing fusion events with ACE2 and thus the following infection.

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