Author: Joana Damas; Graham M. Hughes; Kathleen C. Keough; Corrie A. Painter; Nicole S. Persky; Marco Corbo; Michael Hiller; Klaus-Peter Koepfli; Andreas R. Pfenning; Huabin Zhao; Diane P. Genereux; Ross Swofford; Katherine S. Pollard; Oliver A. Ryder; Martin T. Nweeia; Kerstin Lindblad-Toh; Emma C. Teeling; Elinor K. Karlsson; Harris A. Lewin
Title: Broad Host Range of SARS-CoV-2 Predicted by Comparative and Structural Analysis of ACE2 in Vertebrates Document date: 2020_4_18
ID: 6ne76rh1_18
Snippet: representative species (Fig. S1 ) and 17 sites were variable and not glycosylation sites. First, we assessed the similarity of every contact at the binding interface between two recently solved crystal structures for the human ACE2/SARS-CoV-2 S RBD complex in humans, 6M0J and 6WV1 (13, 21) . Both structures were in agreement except for the position of S19, which was excluded from subsequent analysis (24) . We then generated homology models, and a.....
Document: representative species (Fig. S1 ) and 17 sites were variable and not glycosylation sites. First, we assessed the similarity of every contact at the binding interface between two recently solved crystal structures for the human ACE2/SARS-CoV-2 S RBD complex in humans, 6M0J and 6WV1 (13, 21) . Both structures were in agreement except for the position of S19, which was excluded from subsequent analysis (24) . We then generated homology models, and aligned them to the human ACE2/SARS-CoV-2 S RBD 6M0J
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