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_23
Snippet: The main event that allows virus envelop fusion with the host human cell plasma membrane concerns a conformational change occurring at the SARS-CoV-2 spike protein that converts from pre-fusion conformation to post-fusion conformation after interactions with ACE2 and spike protein cleavage. While SARS-CoV-2 spike protein trimer has been resolved by cryo-em (6vsb.pdb (21); 6vxx.pdb and 6vyb.pdb (22) ), the post-fusion conformation is not available.....
Document: The main event that allows virus envelop fusion with the host human cell plasma membrane concerns a conformational change occurring at the SARS-CoV-2 spike protein that converts from pre-fusion conformation to post-fusion conformation after interactions with ACE2 and spike protein cleavage. While SARS-CoV-2 spike protein trimer has been resolved by cryo-em (6vsb.pdb (21); 6vxx.pdb and 6vyb.pdb (22) ), the post-fusion conformation is not available, yet. According to (11) Coutard et al., protein cleavage at site S1/S2 and S2' produces the division of the spike protein in two subdomains, i.e. the N-ter S-I ectodomain (containing the RBD interacting with ACE2) and the C-ter S-II membrane anchored subdomain, forming the SARS-CoV-2 spike protein in post fusion author/funder. All rights reserved. No reuse allowed without permission.
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