Version 1
: Received: 25 March 2020 / Approved: 26 March 2020 / Online: 26 March 2020 (15:12:34 CET)
Version 2
: Received: 29 March 2020 / Approved: 30 March 2020 / Online: 30 March 2020 (08:25:51 CEST)
How to cite:
Singh, B. Understanding the Role of Key Point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein. Preprints2020, 2020030394. https://doi.org/10.20944/preprints202003.0394.v2
Singh, B. Understanding the Role of Key Point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein. Preprints 2020, 2020030394. https://doi.org/10.20944/preprints202003.0394.v2
Singh, B. Understanding the Role of Key Point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein. Preprints2020, 2020030394. https://doi.org/10.20944/preprints202003.0394.v2
APA Style
Singh, B. (2020). Understanding the Role of Key Point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein. Preprints. https://doi.org/10.20944/preprints202003.0394.v2
Chicago/Turabian Style
Singh, B. 2020 "Understanding the Role of Key Point Mutations in Receptor Binding Domain of SARS-CoV-2 Spike Glycoprotein" Preprints. https://doi.org/10.20944/preprints202003.0394.v2
Abstract
The recent outbreak of novel coronavirus (SARS-CoV-2 or 2019-nCoV) and its spread to the whole world is currently posing one of the major threats to human health and the world economy. It has been suggested that SARS-CoV-2 is similar to SARS-CoV based on the genome sequence comparison. Despite the genomic similarity between SARS-CoV and SARS-CoV-2, the spike glycoprotein and receptor binding domain in SARS-CoV-2 shows considerable difference compared to SARS-CoV, due to the presence of several point mutations. We analyzed the receptor binding domain (RBD) from recently published 3D structure of spike glycoprotein of SARS-CoV-2 and compared with RBD of SARS-CoV. The observations highlight few important features of RBD in the light of the recently published findings from the 3D structures of spike glycoprotein and its complex with human angiotensin-converting enzyme 2 (ACE2) (Yan, R., et al. (2020); Wrapp, D., et al. (2020); Walls, A. C., et al. (2020)).
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Received:
30 March 2020
Commenter:
Bipin Singh
Commenter's Conflict of Interests:
Author
Comment:
Minor corrections:
Abstract:
major threat -> major threats
Results and Discussion
these three point mutations seems->these three point mutations seem
tends-> tend
Leu472, Asn479 and Thr487 critical for-> Leu472, Asn479 and Thr487 are critical
seems-> seem
of non-covalent -> of a non-covalent
volume of cavity-> cavity volume
Commenter: Bipin Singh
Commenter's Conflict of Interests: Author
Abstract:
major threat -> major threats
Results and Discussion
these three point mutations seems->these three point mutations seem
tends-> tend Leu472, Asn479 and Thr487 critical for-> Leu472, Asn479 and Thr487 are critical seems-> seem
of non-covalent -> of a non-covalent volume of cavity-> cavity volume