Selected article for: "binding interface and RBD binding"
Author: Erik Procko
Title: The sequence of human ACE2 is suboptimal for binding the S spike protein of SARS coronavirus 2
  • Document date: 2020_3_17
    • ID: jalijjmg_15
    Snippet: Two ACE2 residues, N90 and T92 that together form a consensus N-glycosylation motif, are 134 notable hot spots for enriched mutations (Fig. 2 and 4A) . Indeed, all substitutions of N90 135 and T92, with the exception of T92S which maintains the N-glycan, are highly favorable for 136 RBD binding, and the N90-glycan is thus predicted to partially hinder S/ACE2 interaction. 137 characterized interface enhance RBD binding, and will be useful for engi.....
    Document: Two ACE2 residues, N90 and T92 that together form a consensus N-glycosylation motif, are 134 notable hot spots for enriched mutations (Fig. 2 and 4A) . Indeed, all substitutions of N90 135 and T92, with the exception of T92S which maintains the N-glycan, are highly favorable for 136 RBD binding, and the N90-glycan is thus predicted to partially hinder S/ACE2 interaction. 137 characterized interface enhance RBD binding, and will be useful for engineering highly 157 specific and tight binders of SARS-CoV-2 S. The molecular basis for how some of these 158 mutations enhance RBD binding can be rationalized from the RBD-bound cryo-EM 159 structure (Fig. 4C ): hydrophobic substitutions of ACE2-T27 increase hydrophobic packing 160 with aromatic residues of S, ACE2-D30E extends an acidic side chain to reach S-K417, and 161 aromatic substitutions of ACE2-K31 contribute to an interfacial cluster of aromatics. 162

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