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_28
Snippet: More in detail, the superimposition performed by using PyMol was leaded by the structural alignment of the RBD of ACE2-SARS-CoV1 (2ajf.pdb) and ACE-2-SARS-CoV-2 (6vw1.pdb, 6lzg.pdb) spike proteins (Fig. 4) , followed by the structure alignment with SARS-CoV-2 spike protein trimer (6vsb.pdb; 6vxx.pdb; 6vyb.pdb). Notably, we obtained an efficient superimposition of the two RBD domains (RMSD lower than 0.5 Ã…) of the human SARS-CoV-1 and SARS-CoV-2 .....
Document: More in detail, the superimposition performed by using PyMol was leaded by the structural alignment of the RBD of ACE2-SARS-CoV1 (2ajf.pdb) and ACE-2-SARS-CoV-2 (6vw1.pdb, 6lzg.pdb) spike proteins (Fig. 4) , followed by the structure alignment with SARS-CoV-2 spike protein trimer (6vsb.pdb; 6vxx.pdb; 6vyb.pdb). Notably, we obtained an efficient superimposition of the two RBD domains (RMSD lower than 0.5 Ã…) of the human SARS-CoV-1 and SARS-CoV-2 spike proteins also due to their high percentage of identical residues (> 75%).
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