Selected article for: "Î1 helix and long loop"
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_14
    Snippet: whereas residues at the interface periphery or in the substrate-binding cleft are 128 mutationally tolerant (Fig. 4A) . The region of ACE2 surrounding the C-terminal end of the 129 ACE2 α1 helix and β3-β4 strands has a weak tolerance of polar residues, while amino acids 130 at the N-terminal end of α1 and the C-terminal end of α2 prefer hydrophobics (Fig. 4B) , 131 likely in part to preserve hydrophobic packing between α1-α2. These discret.....
    Document: whereas residues at the interface periphery or in the substrate-binding cleft are 128 mutationally tolerant (Fig. 4A) . The region of ACE2 surrounding the C-terminal end of the 129 ACE2 α1 helix and β3-β4 strands has a weak tolerance of polar residues, while amino acids 130 at the N-terminal end of α1 and the C-terminal end of α2 prefer hydrophobics (Fig. 4B) , 131 likely in part to preserve hydrophobic packing between α1-α2. These discrete patches 132 contact the globular RBD fold and a long protruding loop of the RBD, respectively. 133

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