Author: Ratul Chowdhury; Costas D Maranas
Title: Biophysical characterization of the SARS-CoV2 spike protein binding with the ACE2 receptor explains increased COVID-19 pathogenesis Document date: 2020_3_31
ID: lotyldfd_13
Snippet: Sequence alignment of the three RBD sequences reveal a conserved motif in all three sequences (see Figure 5 ). Further inspection of the sequence alignment reveals that all of the three other conserved binding motifs for the ACE2 hotspot residues (Thr27, Asp38, and Gln42) have a key glycine (and rarely alanine) which presumably offers a hinge to orient a neighboring polar residue to bind to a specific ACE2 residue. The copyright holder for this p.....
Document: Sequence alignment of the three RBD sequences reveal a conserved motif in all three sequences (see Figure 5 ). Further inspection of the sequence alignment reveals that all of the three other conserved binding motifs for the ACE2 hotspot residues (Thr27, Asp38, and Gln42) have a key glycine (and rarely alanine) which presumably offers a hinge to orient a neighboring polar residue to bind to a specific ACE2 residue. The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.30.015891 doi: bioRxiv preprint
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