Author: Mushtaq Hussain; Nusrat Jabeen; Anusha Amanullah; Ayesha Ashraf Baig; Basma Aziz; Sanya Shabbir; Fozia Raza
Title: Structural Basis of SARS-CoV-2 Spike Protein Priming by TMPRSS2 Document date: 2020_4_22
ID: 34ljq0qt_18
Snippet: Whereas, at the second cleavage site (Arg815/Ser816), out of the three residues of catalytic triad, His296 and Ser441 established hydrogen bond interactions with Pro809, Lys814 and Ser810 of the SARS-CoV-2 spike protein (Table 1 ; Figure 3D ). Ser810 also formed a hydrogen bond and hydrophobic interaction with Ser460, substrate binding site, and His296, catalytic site of TMPRSS2, respectively (Table 1 ; Figure 3D ). Since the functionally importa.....
Document: Whereas, at the second cleavage site (Arg815/Ser816), out of the three residues of catalytic triad, His296 and Ser441 established hydrogen bond interactions with Pro809, Lys814 and Ser810 of the SARS-CoV-2 spike protein (Table 1 ; Figure 3D ). Ser810 also formed a hydrogen bond and hydrophobic interaction with Ser460, substrate binding site, and His296, catalytic site of TMPRSS2, respectively (Table 1 ; Figure 3D ). Since the functionally important residues of author/funder. All rights reserved. No reuse allowed without permission.
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